Academic literature on the topic 'Whey protein ratio'

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Journal articles on the topic "Whey protein ratio"

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Venter, B. G., and A. E. J. McGill. "The functional properties, modification and utilization of whey proteins." Suid-Afrikaanse Tydskrif vir Natuurwetenskap en Tegnologie 5, no. 2 (March 18, 1986): 98–104. http://dx.doi.org/10.4102/satnt.v5i2.983.

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Whey protein has an excellent nutritional value and exhibits a functional potential. In comparison with certain other food proteins, the whey protein content of essential amino acids is extremely favourable for human consumption. Depending on the heat-treatment history thereof, soluble whey proteins with utilizable functional properties, apart from high biological value, true digestibility, protein efficiency ratio and nett protein utilization, can be recovered. Various technological and chemical recovery processes have been designed. Chemically and enzymatically modified whey protein is manufactured to obtain technological and functional advantages. The important functional properties of whey proteins, namely hydration, gelation, emulsifying and foaming properties, are reviewed.
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Hejtmánková, V. Pivec, E. Trnková, and H. Dragounová. " Differences in the composition of total and whey proteins in goat and ewe milk and their changes throughout the lactation period." Czech Journal of Animal Science 57, No. 7 (July 10, 2012): 323–31. http://dx.doi.org/10.17221/6007-cjas.

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This study was conducted to evaluate changes in composition of whey proteins of Czech White Short-haired goat and East Friesian ewe milk and their comparison throughout lactation. Some differences in composition between ewe and goat milk were found. The results showed that the mean total protein (%), whey protein (g/100 g), and β-lactoglobulin (β-Lg, g/100 g) contents of goat milk were 2.75, 0.433, and 0.119 respectively and of ewe milk 6.36, 1.11, and 0.732 respectively. The contents of total protein as well as acid whey proteins in goat milk were nearly constant throughout the lactation period and fluctuated around the mean value while the contents of total protein as well as acid whey proteins in ovine milk were dependent on the period of lactation. The total protein content in ovine milk continuously increased during the lactation period. A higher content of ovine acid whey proteins was noticed at the beginning and in the final period of lactation. The average ratio of whey to total protein was 15.8  2.61% in goat milk and 17.4  2.68% in ewe milk and ranged from 13.0 to 20.4% in goat and from 14.0 to 20.8% in ewe milk. The total contents of two major whey proteins. α-lactalbumin and β-lactoglobulin (α-La + β-Lg = AG), averaged 87% of total whey protein, 92% in ovine milk. The main component of acid whey proteins in goat milk was α-La while in ovine milk the main component of acid whey proteins was β-Lg, however, at the end of the lactation period the content of β-Lg for both kinds of milk increased steeply, and the β-Lg/α-La ratio reached a maximum value of 1.94 in goat milk and of 9.74 in ewe milk. In addition, goat milk contains a similar amino acid profile to ewe milk but the amino acid pattern in whey proteins differs from that in milk. Total essential amino acids were approximately 40% of the total amino acids in goat and ewe milk as well as in goat and ewe whey.    
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Thu, Tran Le. "EVALUATION OF THE INFLUENCE OF A VARYING MOLAR RATIO OF SODIUM DODECYL SULFATE TO WHEY PROTEIN ISOLATE ON THE STABILITY OF THE WHEY PROTEIN EMULSIONS." Vietnam Journal of Science and Technology 55, no. 5A (March 24, 2018): 26. http://dx.doi.org/10.15625/2525-2518/55/5a/12175.

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In combination with the Lumifuge centrifugation and Zeta potential apparatuses, the influence of a varying molar ratio of Sodium Dodecyl Sulfate (SDS) to Whey Protein Isolate (WPI) on the stability of the whey protein emulsions at pH 4 and pH 5.5 is observed. Two whey protein stabilized emulsions were prepared by homogenizing 20 wt. % soybean oil and 80 wt. % whey protein solutions (0.5 wt.% whey protein in buffer, pH 4 and pH 5.5) at room temperature.By observation, the droplets are weakly flocculated at a ratio of SDS to whey protein of 256. This shows that there is a strong electrostatic repulsion between the emulsion droplets if much surfactant is adsorbed to the protein molecules, which prevents them from aggregating. The magnitude of the measured zeta potentials explained the stability of the emulsion at pH 4 as well as the emulsion at pH 5.5 is ensured at SDS to whey protein ratio equal to 256. The results of the transmission profile by Lumifuge separation analyzer at different time and at 3000 rpm (1200 g) elucidated that the stability of the whey protein emulsion at pH 4 and 5.5 is obtained upon dilution with SDS-WPI ratio of 256.
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Al-Hatim, Raqad R., Ali K. Al-Rikabi, and Amal K. Ghadban. "The Physico-Chemical Properties of Bovine and Buffalo Whey Proteins Milk by Using Ultrafiltration Membrane Technology." Basrah J. Agric. Sci. 33, no. 1 (June 27, 2020): 122–34. http://dx.doi.org/10.37077/25200860.2020.33.1.10.

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The current study aims to prepare whey from bovine and buffalo fresh milk to make three types of cheese, namely: thermal, acidic and enzymatic. Afterward, whey proteins have been separated, then the concentration process of whey proteins has been conducted by using ultrafiltration membrane technology. Through the previous step, two products have been obtained; first, concentrated whey proteins which is called (Retentate), while the other is called (Permeate). Applying rotary evaporator, whey proteins are concentrated and then drying in two methods: spray-drying and freeze-drying in a form of white and soft powder. The chemical composition has been studied at each phase. The results show the separation, purification, and concentration of bovine and buffalo whey proteins by using ultrafiltration membrane technology. The results show that buffalo whey proteins produced by the method of enzymatic and dried with spray-drying are better than bovine whey protein. Finally, the results show a low ratio of lactose, salts and moisture content at the stages of filtration and concentration. The results present a high proportion of protein to 80 .and low ratio lactose and salt.
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Chalermthai, Chan, Bastidas-Oyanedel, Taher, Olsen, and Schmidt. "Preparation and Characterization of Whey Protein-Based Polymers Produced from Residual Dairy Streams." Polymers 11, no. 4 (April 19, 2019): 722. http://dx.doi.org/10.3390/polym11040722.

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The wide use of non-biodegradable, petroleum-based plastics raises important environmental concerns, which urges finding alternatives. In this study, an alternative way to produce polymers from a renewable source—milk proteins—was investigated with the aim of replacing polyethylene. Whey protein can be obtained from whey residual, which is a by-product in the cheese-making process. Two different sources of whey protein were tested: Whey protein isolate (WPI) containing 91% protein concentration and whey protein concentrate (WPC) containing 77% protein concentration. These were methacrylated, followed by free radical polymerization with co-polymer poly(ethylene glycol) methyl ether methacrylate (PEGMA) to obtain polymer sheets. Different protein concentrations in water (11–14 w/v%), at two protein/PEGMA mass-ratios, 20:80 and 30:70, were tested. The polymers made from WPI and WPC at a higher protein/PEGMA ratio of 30:70 had significantly better tensile strength than the one with lower protein content, by about 1–2 MPa (the best 30:70 sample exhibited 3.8 ± 0.2 MPa and the best 20:80 sample exhibited 1.9 ± 0.4 MPa). This indicates that the ratio between the hard (protein) and soft (copolymer PEGMA) domains induce significant changes to the tensile strengths of the polymer sheets. Thermally, the WPI-based polymer samples are stable up to 277.8 ± 6.2 °C and the WPC-based samples are stable up to 273.0 ± 3.4 °C.
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Agarkova, Eugeniya, Alexandr Kruchinin, Nikita Zolotaryov, Nataliya Pryanichnikova, Zinaida Belyakova, and Tatyana Fedorova. "Processing cottage cheese whey components for functional food production." Foods and Raw Materials 8, no. 1 (February 26, 2020): 52–59. http://dx.doi.org/10.21603/2308-4057-2020-1-52-59.

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Introduction. The study offers a new rational approach to processing cottage cheese whey and using it as a highly nutritional functional ingredient in food production. We proposed a scientifically viable method for hydrolyzing cottage cheese whey with enzyme preparations of acid proteases from Aspergillus oryzae with an activity of 400 units/g and a pH range of 3.0 to 5.0. Study objects and methods. Pre-concentrated whey was enzymatically hydrolyzed at 30°C, 40°C, and 50°C for 60 to 180 min (pH 4.6). Non-hydrolyzed whey protein concentrates were used as a control. The amount of enzyme preparation was determined by calculation. All hydrolysate samples showed an increase in active acidity compared to the control samples. Further, we conducted a full-factor experiment with three levels of variation. The input parameters included temperature, duration of hydrolysis, and a substrate-enzyme ratio; the output parameters were the degree of hydrolysis and antioxidant capacity. Results and discussion. The experiment showed the following optimal parameters for hydrolyzing cottage cheese whey proteins with the enzyme preparation of proteases produced by Aspergillus oryzae: temperature – 46.4°C; duration – 180 min; and the amount of enzyme preparation – 9.5% of the protein content. The antioxidant capacity was 7.51 TE mmol/L and the degree of hydrolysis was 17.96%. Conclusion. Due to its proven antioxidant capacity, the whey protein hydrolysate obtained in the study can be used as a functional food ingredient.
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Kunz, Clemens, and Bo Lönnerdal. "Re-evaluation of the whey protein/casein ratio of human milk." Acta Paediatrica 81, no. 2 (February 1992): 107–12. http://dx.doi.org/10.1111/j.1651-2227.1992.tb12184.x.

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VAN BERESTEIJN, EMERENTIA C. H., ROGER A. PEETERS, JAAP KAPER, RON J. G. M. MEIJER, ARJAN J. P. M. ROBBEN, and DANIËL G. SCHMIDT. "Molecular Mass Distribution Immunological Properties Nutritive Value of Whey Protein Hydrolysates." Journal of Food Protection 57, no. 7 (July 1, 1994): 619–25. http://dx.doi.org/10.4315/0362-028x-57.7.619.

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Whey protein concentrate was hydrolyzed using the technical food-grade enzyme Corolase 7092 in order to abolish the allergenicity of whey proteins. The immunological properties of the hydrolysates were tested in vitro with a human-immunoglobulin E (human-IgE) enzyme-linked immunosorbent assay (ELISA) using sera obtained from children allergic to milk proteins and in vivo with a mouse-rat heterologous passive cutaneous anaphylactic test and an anaphylactic shock test in mice. The protein efficiency ratio, determined in young growing rats, was compared to that of casein. Ultrafiltration of the hydrolysates appeared to be necessary to obtain a hypo-allergenic product. The minimal molecular mass to elicit immunogenicity and allergenicity of whey protein hydrolysates appeared to be between 3,000 and 5,000 Da, so the molecular weight cut-off value of the filters required must be in this range. Although there was no evidence that extensively hydrolyzed whey protein is nutritionally inferior to casein, the slightly bitter taste might reduce food intake.
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Xia, Ze Ying, and Ming Xia. "Orthogonal Optimization of Enzymatic Hydrolysis of Whey Protein." Advanced Materials Research 550-553 (July 2012): 1556–60. http://dx.doi.org/10.4028/www.scientific.net/amr.550-553.1556.

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Objective The study proposed an efficient and economic approach to hydrolyze whey protein isolate. Methods Using trypsin to hydrolyze the whey protein, this study investigated the influences of pH, hydrolysis temperature, enzyme-substrate ratio (E/S) and hydrolysis duration on the process of enzymatic hydrolysis. The orthogonal test method was used to design the experiments of the study. Result The optimized conditions of enzymatic hydrolysis were pH8, hydrolysis temperature 40°C,5% of E/S, and hydrolysis duration 2 hours. The hydrolysis degree was 26.5%. Conclusion The parameters identified from this study can benefit the development of whey protein.
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Miralles, B., B. Bartolomé, L. Amigo, and M. Ramos. "Comparison of Three Methods to Determine the Whey Protein to Total Protein Ratio in Milk." Journal of Dairy Science 83, no. 12 (December 2000): 2759–65. http://dx.doi.org/10.3168/jds.s0022-0302(00)75171-x.

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Dissertations / Theses on the topic "Whey protein ratio"

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Martin, François. "Impact des shémas technologiques de fabrication, de la formulation et du veillissement sur l'état des protéines et les propriétés technofonctionnelles des poudres protéiques laitières." Electronic Thesis or Diss., Rennes, Agrocampus Ouest, 2022. http://www.theses.fr/2022NSARB363.

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Ce projet de thèse CIFRE a eu pour objectif de mieux cerner les évolutions de structure et de propriétés fonctionnelles subies par les concentrés protéiques laitiers au cours de leur élaboration, en lien avec les paramètres de procédés appliqués. L’influence du schéma technologique de fabrication, de la base de mélange (eau vs perméat d’ultrafiltration de lait) et de la formulation (différents ratios Caséines/Protéines solubles) sur les caractéristiques physico-chimiques, la susceptibilité enzymatique, les propriétés physiques des poudres et les propriétés de réhydratation qui en découlent ont notamment été évalués. Ce travail a montré que l’étude des milieux concentrés bousculait les connaissances conventionnelles sur les mécanismes de dénaturation/agrégation thermique des protéines obtenues dans le lait. En milieu plus concentré, le chauffage induit une augmentation du taux de dénaturation/agrégation des protéines solubles (Ps) ainsi que la formation privilégiée de complexes caséines ¿ / Ps à la surface des micelles. Ces deux phénomènes modifient significativement les propriétés de coagulation enzymatique des produits obtenus en perturbant notamment la réorganisation des « clusters » de para-micelles de caséines. Ce travail a également permis d’établir un lien clair entre le taux de dénaturation/agrégation des Ps et l’augmentation de la viscosité des concentrés en fonction du ratio cas/Ps. Finalement, cette étude a mis en évidence que les propriétés physiques des poudres étaient plus impactées par leur formulation que par le schéma technologique mis en œuvre
The objective of this PhD project (CIFRE) aimed to assess and understand the changes in structure and functional properties undergone by milk protein concentrates during their production, in relation to the process parameters applied. We investigated the influence of the technological process schemes, the standardization in osmosed water or ultrafiltration permeate and the formulation (different casein/whey protein ratios) on the physicochemical characteristics, the enzymatic susceptibility, the physical properties of the powders and the resulting rehydration properties. This work showed that the study of concentrated solutions overturned conventional knowledge on the mechanisms of thermal denaturation/aggregation of proteins obtained in milk.In more concentrated solutions, heat treatment induces an increase in the level of denaturation/aggregation of whey proteins (WP) as well as the privileged formation of ¿ casein/WP complexes on the surface of micelles. These two phenomena significantly modify the enzymatic coagulation properties of the rehydrated powders by disturbing the reorganization of the casein paramicelles clusters. This work also established a clear link between the level of denaturation/aggregation of WP and the increase in the viscosity of the concentrates as a function of the casein/WP ratio. Finally, this study showed that the physical properties of the powders were more affected by their formulation than by the technological scheme used
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Wei, Ting. "A dairy-based beverage development by alpha-lactalbumin/beta-lactoglobulin ratio adjustment for dysphagia patients." Thesis, Kansas State University, 2014. http://hdl.handle.net/2097/17649.

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Master of Science
Department of Food Science
Karen A. Schmidt
People who suffer from swallowing disorders are diagnosed with dyphasgia. The beverage for the dyphagia patients should have the apparent viscosity in the range of nectar-like (51 to 350 mPa•s) or honey-like (351 to 1750 mPa•s). Due to the swallowing problems, dysphagia patients usually consume beverages slowly. Thus, the apparent viscosity of beverage for such patients should be high enough to be in the suitable range during the entire time of consumption. Three ratios of α-lactalbumin (α-la)/β-lactoglobulin (β-lg) (3:8, 1:1 and 8:3) were used to prepare the milk systems. These ratio adjusted milk systems were either processed at 70, 80, and 90ºC for 30 min or at 25ºC, and cooled to 25 ± 1ºC. After the process was completed, the milk systems were set quiescently 120 min at 25 ±1ºC. Physical and chemical properties were assessed at various time. For the milk systems at 0 min, the apparent viscosity increased in all 90°C processed-samples, and the increase was in the order of 8:3 (15.96%), 1:1 (6.38%) and 3:8 (2.11%) compared with the 25ºC samples at each ratio. When the milk systems set for 120 min, apparent viscosity increased slightly by 3.7%. The maximum apparent viscosity was 2.18 mPa•s, which was less than nectar-like. Therefore, xanthan gum was added at 0.15 w/w % to enhance rheological properties of the milk systems. α-La/β-lg ratio adjusted milk systems either with or without xanthan gum were prepared, and processed at 90ºC or 25ºC, and cooled to 25 ± 1ºC. Apparent viscosity increased by 48.61 and 89.61% in 3:8 and 8:3 milk systems, respectively for those at 0.15% xanthan gum concentration and processed at 90ºC compared with at 25ºC. Apparent viscosity of 8:3 milk systems at xanthan gum concentration of 0.15% processed at 90°C was 58.7 ± 2.12 mPa•s which was within the nectar-like range. When the samples were set for 120 min, no changes were found in the apparent viscosity of the milk systems. If the rheological properties of the milk systems can be controlled by ingredients interactions, this can be used to develop nutritious products with different forms for dysphagia patients.
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Nery-Diez, Ana Cláudia Coelho 1980. "Efeito do consumo de proteina do soro do leite bovino, parcialmente hidrolisada e da atividade fisica em proteases intestinais do rato." [s.n.], 2007. http://repositorio.unicamp.br/jspui/handle/REPOSIP/254488.

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Orientador: Jaime Amaya-Farfan
Dissertação (mestrado) - Universidade Estadual de Campinas, Faculdade de Engenharia de Alimentos
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Resumo: As proteínas do soro do leite apresentam propriedades fisiológicas, funcionais e nutricionais diferentes que resultam na modulação ou melhoramento de funções bioquímicas e fisiológicas, aumentando a resistência e protegendo o organismo contra infecções ou retardando certos processos patológicos, assim como melhorando o desempenho físico. Estudos têm demonstrado melhoras em parâmetros bioquímicos e físicos proporcionados por estas proteínas. Assim, considerou-se de interesse investigar algumas das possíveis alterações ou efeitos fisiológicos, provocados pela ingestão de fonte protéica de alto peso molecular (isolado do soro do leite) e um hidrolisado enzimático dessa proteína. Além disso, levou-se em consideração o efeito da atividade física em ratos treinados em esteira, na atividade catalítica de proteases intestinais como: glutaminase, leucina-aminopeptidase, quimotripsina e tripsina e verificou-se também a possível absorção de peptídeos que constituem o hidrolisado, no intestino delgado. Na análise das atividades enzimáticas observou-se que o consumo da proteína hidrolisada promoveu diminuição da atividade da enzima glutaminase intestinal de 25 a 29%, em relação à atividade produzida pelas proteínas intactas (isolado e caseína). O treinamento, porém, teve como efeito aumentar a atividade glutaminase entre 27 e 32% para cada uma das dietas, exceto para o hidrolisado, que permaneceu sem alteração. A exaustão, por outro lado, resultou em diminuição da atividade glutaminase intestinal para quase todas as dietas (média aproximada de 30%). Na avaliação das enzimas presentes no lúmen intestinal, as atividades das três proteases, leucina-aminopeptidase, quimotripsina e tripsina, foram encontradas mais elevadas na fração do jejuno, em comparação ao íleo. Foi observada uma aparente inibição enzimática da tripsina na fração jejunal pela presença de caseína. Para verificar a possibilidade de absorção de peptídeos inteiros, foi realizada uma análise in vitro com os intestinos delgados. O intestino fresco extraído foi infundido com uma suspensão de cada proteína e incubado em solução fisiológica por duas horas, na temperatura de 37°C. Após, tal procedimento, os perfis de aminoácidos e de peptídeos perfusados foram obtidos por métodos cromatográficos e eletroforéticos. Neste estudo, pode-se constatar que houve maior passagem de aminoácidos nos intestinos delgados dos grupos sedentários-exaustos e treinados, que foram infundidos com o hidrolisado e nos grupos sedentários e treinados, que foram infundidos com isolado. Em relação aos diferentes níveis de atividade física, os animais treinados, alimentados com ambas as dietas, isolado e seu proteolisado, tiveram maior passagem de aminoácidos. Conclui-se que o consumo da proteína parcialmente hidrolisada não afetou de igual forma a atividade das três proteases, tripsina, quimotripsina e leucina-aminoeptidase, sendo que o treinamento e o hidrolisado, conjuntamente, redundaram em diminuição da atividade da quimotripsina, enquanto que a atividade da glutaminase foi visivelmente diminuída pela combinação da exaustão e o consumo do hidrolisado. Por sua vez, foi possível evidenciar a passagem de peptídeos do hidrolisado, do interior, para o exterior do jejuno perfusado do rato
Abstract: The whey protein offers various physiological, functional and nutritional properties that result in the modulation or improvement of physiological and biochemical functions, thus protecting the body against infections and delaying the onset of certain pathological processes, as well as improving the physical performance. Researchers have attributed to these proteins benefits such as the improvement of biochemical and physical parameters of the exercising animal. Therefore, it was considered of interest investigate some of the possible alterations resulting from the ingestion of the milk whey proteins (whey protein isolate) as the only source of high-molecular weight protein, as compared to an intermediate-degree enzymatic hydrolyzate of this protein and the casein standard. Moreover, the effect of the physical activity on the catalytic activity of the intestinal proteases glutaminase, leucine-aminopeptidase, chymotrypsin and trypsin, of rats trained in the treadmill was taken as an additional variable. Moreover, the possible absorption of constituent peptides of the hydrolyzate from the small intestine was investigated. In the analysis of the enzymatic activities it was observed that the consumption of the hydrolyzed protein prompted a reduction of the activity of the intestinal enzyme glutaminase by 25 to 29%, in relation to the activity produced by the unbroken proteins (isolate and casein). Physical training, however, had the effect of increasing the activity of glutaminase between 27 and 32% for each one of the diets, except for the hydrolyzate, which remained unaltered. Exhaustion, on the other hand, resulted in the reduction of the intestinal activity glutaminase for most of the diets (mean of ~30%). Assessment of the enzymes present in the intestinal lumen, the activities of three proteases, leucine-aminopeptidase, chymotrypsin and trypsin, were higher in the jejunal fraction, in comparison to the ileum. An apparent enzymatic inhibition of trypsin occurred in the jejunal fraction in the presence of casein. In order to verify the possibility of absorption of whole peptides, fresh intestinal fractions were infused with suspensions of each protein and incubated in physiological solution for two hours, at 37°C. After, such process the amino acid and peptide profiles were determined by chromatographic procedures. It was observed that a greater outflow amino acids occurred in the intestines sedentary-exhaust and trained group that were infused with the hydrolyzate, and in the sedentary and trained group that were infused with whey protein isolate. With regard to the effect of the different levels of physical activity, the animals that underwent training, fed with either of the diets, isolate or its hydrolyzate, had greater amino acid outflow than the sedentary animals. It is concluded that consumption of the hydrolyzate did not affect equally the activity of the three proteases, trypsin, chymotrypsin and leucine-aminopeptidase, noticing that a combination between training and the hydrolyzate caused a decrease of the activity of chymotrypsin, whereas the activity of glutaminase was clearly diminished by a combination between exhaustion and consumption of the hydrolyzate. Evidence has been presented showing that infusion of the hydrolyzate into the small intestine of the rat results in the passage of peptides from the interior to the exterior of the intestinal wall
Mestrado
Nutrição Experimental e Aplicada à Tecnologia de Alimentos
Mestre em Alimentos e Nutrição
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Leão, Carolina Cauduro Bensabath Carneiro. "Composiçõa bioquimica dos musculos cardíaco e gastrocnemio, figado e sangue de ratos alimentados com proteina intacta e hidrolisada do soro do leite e submetidos a atividade fisica." [s.n.], 2009. http://repositorio.unicamp.br/jspui/handle/REPOSIP/254452.

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Orientador: Jaime Amaya Farfan
Dissertação (mestrado) - Universidade Estadual de Campinas, Faculdade de Engenharia de Alimentos
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Mestrado
Nutrição Experimental e Aplicada à Tecnologia de Alimentos
Mestre em Alimentos e Nutrição
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Amatayakul, Thanut. "The improvement of physical properties of yoghurts by varying casein/whey protein ratio and EPS-producing starter cultures." Thesis, 2005. https://vuir.vu.edu.au/15558/.

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The overall objective of this study was to investigate effects of variation in casein to whey protein ratios and types of exopolysaccharide producing starter cultures on physical properties of yoghurts made at 9% and 14% total solids during 28 days of storage at 4°C. There are three main parts of this research: a preliminary study, a comparative study of three methods for determination of syneresis and the studies on physical properties of yoghurts made with various casein to whey protein ratios using non-exopolysaccharide or exopolysaccharide-producing starter cultures.
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Book chapters on the topic "Whey protein ratio"

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Di Maso, Matteo, Monica Ferraroni, Pasquale Ferrante, Serena Delbue, and Federico Ambrogi. "Longitudinal profile of a set of biomarkers in predicting Covid-19 mortality using joint models." In Proceedings e report, 191–96. Florence: Firenze University Press, 2021. http://dx.doi.org/10.36253/978-88-5518-461-8.36.

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In survival analysis, time-varying covariates are endogenous when their measurements are directly related to the event status and incomplete information occur at random points during the follow-up. Consequently, the time-dependent Cox model leads to biased estimates. Joint models (JM) allow to correctly estimate these associations combining a survival and longitudinal sub-models by means of a shared parameter (i.e., random effects of the longitudinal sub-model are inserted in the survival one). This study aims at showing the use of JM to evaluate the association between a set of inflammatory biomarkers and Covid-19 mortality. During Covid-19 pandemic, physicians at Istituto Clinico di Città Studi in Milan collected biomarkers (endogenous time-varying covariates) to understand what might be used as prognostic factors for mortality. Furthermore, in the first epidemic outbreak, physicians did not have standard clinical protocols for management of Covid-19 disease and measurements of biomarkers were highly incomplete especially at the baseline. Between February and March 2020, a total of 403 COVID-19 patients were admitted. Baseline characteristics included sex and age, whereas biomarkers measurements, during hospital stay, included log-ferritin, log-lymphocytes, log-neutrophil granulocytes, log-C-reactive protein, glucose and LDH. A Bayesian approach using Markov chain Monte Carlo algorithm were used for fitting JM. Independent and non-informative priors for the fixed effects (age and sex) and for shared parameters were used. Hazard ratios (HR) from a (biased) time-dependent Cox and joint models for log-ferritin levels were 2.10 (1.67-2.64) and 1.73 (1.38-2.20), respectively. In multivariable JM, doubling of biomarker levels resulted in a significantly increase of mortality risk for log-neutrophil granulocytes, HR=1.78 (1.16-2.69); for log-C-reactive protein, HR=1.44 (1.13-1.83); and for LDH, HR=1.28 (1.09-1.49). Increasing of 100 mg/dl of glucose resulted in a HR=2.44 (1.28-4.26). Age, however, showed the strongest effect with mortality risk starting to rise from 60 years.
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Räihä, Niels C. R. "Protein Quantity and Whey-Casein Ratio in Infant Formulas." In Protein and Non-Protein Nitrogen in Human Milk, 137–44. CRC Press, 2019. http://dx.doi.org/10.1201/9780367812805-10.

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Jacob Nte, Iyakutye, and Hollinshead Holly Gunn. "Cysteine in Broiler Poultry Nutrition." In Biosynthesis [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.97281.

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The SAAs are limiting in the major poultry feed ingredients, ranking first and fifth in soya bean meal and maize, respectively. Feed ingredients rich in protein, in particular and other nutrients, enhance Energy supply and protein accretion. Modern commercial broilers have reduced maintenance needs and high amino acid requirements, and are more responsive to protein (amino acids) than energy. Cysteine is a semi-essential amino acid belonging to the SAAs. It plays essential roles in protein synthesis, structure and function, causing growth depressing effects in broiler chicks when there is methionine:cysteine imbalance. Genetically predetermined amino acid sequences in proteins are essential for production of adequate quantities of meat, milk and eggs. Therefore, ideal amino acid ratios which conform to the requirements of broilers should be utilized. In nutrition, amino acids are equivalent to proteins, hence the shift in focus from proteins to individual amino acids, expressed as ideal ratios to lysine. The SAAs are practically relevant and have critical nutritional roles in animal nutrition with over 90% production being used to fortify animal (particularly poultry) diets. A balance in the methionine:cysteine ratio is necessary to ensure efficient utilization of the SAAs for proper growth and development in broiler poultry.
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Bekele, Birhanu. "Innovative Approach of Cheese Making from Camel Milk: A Review." In Dairy Processing - From Basics to Advances [Working Title]. IntechOpen, 2022. http://dx.doi.org/10.5772/intechopen.108700.

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Camel milk contains all essential important components of human diet and generates cash, ensures food security, and provides health benefits. Compared to cow milk, camel milk has higher levels of whey protein, lower levels of αs1-casein, larger size of κ-casein, and a very low κ- to β-casein ratio. As a result, the technical characteristic of the acidic or enzymatic coagulation process of camel milk for cheese making is affected by all these factors. Camel milk cheese is a recent product that enters into both the domestic and global milk product markets. Cheese made from camel milk can have processing issues and be of lower quality if it is produced using the same technology as dairy products made from bovine milk. To maximize the possibility of manufacturing cheese from camel milk, various trials were conducted over time utilizing different methods. This chapter reviews the advancements in making cheeses from camel milk using starter cultures and coagulants. Furthermore, the relevant studies describing the fortification of camel milk with ingredients for cheese making are included.
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Mohi Alddin Abdulrahman, Nasreen. "Microalgae and Fish Nutrition." In Progress in Microalgae Research: A path for shaping sustainable futures [Working Title]. IntechOpen, 2022. http://dx.doi.org/10.5772/intechopen.105028.

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Fish has long been a source of “rich food for poor people” and has played an important role in increasing food security and nutrition in developing countries. Because various chemicals in algae can have confusing effects, the results of experimental research can be difficult to understand. Algae has been associated with strengthening immune systems, lipid metabolism, antiviral and antibacterial action, improved gut function, stress resistance besides providing a source of protein, amino acids, fatty acids, vitamins and minerals, and other biologically active phytochemicals in cattle and aquaculture feeds, even when used in modest amounts. The addition of algae to the fish diet modified the growth performance of the fish, causing it to improve. Its use resulted in a decrease in feed conversion ratio expenses, which plays an important part in determining aquaculture costs, an increase in feed efficiency ratio, and a decrease in feed conversion ratio. In accordance with the findings of chemical composition, various statements were acquired wherein the high proportion of algae significantly affects the protein and fat ratio. The outcomes demonstrated that algae could be a decent option as an additive for fish feed.
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Simpson, Stephen J., and David Raubenheimer. "The Geometry of Human Nutrition." In The Nature of Nutrition. Princeton University Press, 2012. http://dx.doi.org/10.23943/princeton/9780691145655.003.0010.

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This chapter explores the methods of nutritional geometry on the modern human diet, applying the geometric approach to an analysis of a key aspect of human nutrition: the topical subject of human obesity. This analysis leads to three conclusions. First, the available evidence suggests that humans can regulate macronutrient intake, but that the intake target contains a built-in component for fat storage. Failure to use this stored fat promotes obesity. Second, when humans are faced with imbalanced diets, protein intake is prioritized. When the ratio of protein to carbohydrate in the diet is lower than optimal, it is easier to gain the required amount of protein—and hence overconsume fat and carbohydrate—when foods are high in energy density, present in great variety, and easily available throughout the day. Lastly, the regulation of nutrient intake in humans has evolved “assuming” a higher level of energetic expenditure than is usual today.
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Santacruz-Vázquez, Claudia, and Verónica Santacruz-Vázquez. "Microencapsulation of acachul (Ardisia Compressa) extract by spray drying using diferente polymeric materials as encapsulating agents." In CIERMMI Women in Science Engineering and Technology TXV, 147–59. ECORFAN, 2021. http://dx.doi.org/10.35429/h.2021.6.147.159.

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The microencapsulation process is a technique whose purpose is to protect liquid, solid and gaseous compounds susceptible to thermal, light or oxidative deterioration, among other factors. The particular substance may be individually coated with an encapsulating material to protect it from the environment, from the reaction with other compounds or to prevent oxidation reactions from light or oxygen present in its surroundings. There is a wide variety of biopolymeric materials used as barrier materials for encapsulation. Among the materials that serve as encapsulating or entraining agents are carbohydrates, lipids, proteins and polymers, while the active or encapsulated compounds may be antimicrobials, pigments, vitamins, minerals or microorganisms. Therefore there is a need to find the best option, to encapsulate the desired active ingredients using different biopolymeric materials as barrier materials. Whence, in the present work, the effect and characteristics from acachul (Ardisia Compressa) pigments were determined, encapsulated them using maltodextrin, gum arabic and a combination of gum arabic- maltodextrin in a 1:1 ratio as encapsulating agents. Determining that acachul (Ardisia Compressa) pigments were better encapsulated when maltodextrin was utilized as the encapsulating agent.
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Garg, Rajesh K. "Metabolic Syndrome." In The Brigham Intensive Review of Internal Medicine, 527–31. Oxford University Press, 2014. http://dx.doi.org/10.1093/med/9780199358274.003.0053.

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Bone is a dynamic and complex organ that undergoes constant remodeling. It consists of an organic matrix (collagen and some noncollagenous proteins), minerals (calcium and phosphate in hydroxyapatite crystals), and water. Normally bone mass is maintained by a tight coupling of bone breakdown by osteoclasts followed by bone formation by osteoblasts. This chapter summarizes three metabolic bone diseases. Osteoporosis is characterized by a decreased bone mass with a normal mineral-to-matrix ratio and superimposed skeletal fragility and fractures; osteomalacia occurs when there is a reduced mineralization of the matrix; and Paget's disease is a disorder in which there is excessive, disorganized bone resorption and formation.
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Johnson, Derek, and Manisha Patel. "Metabolic and Redox Alterations by Ketogenic Diets." In Ketogenic Diet and Metabolic Therapies, edited by Susan A. Masino, Detlev Boison, Dominic P. D’Agostino, Eric H. Kossoff, and Jong M. Rho, 364–70. Oxford University Press, 2022. http://dx.doi.org/10.1093/med/9780197501207.003.0030.

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When there is a shift from glucose utilization (glycolysis) resulting from carbohydrate-restrictive diets like the ketogenic diet, metabolic changes occur, and acetyl-CoA is instead derived from the alternative parallel processes of gluconeogenesis and fatty acid oxidation. Under these conditions, several antioxidant pathways are amplified, including the transcription factor Nrf2, the Forkhead box pathway, the NAD+:NADH ratio, and uncoupling proteins. Additionally, amino acid metabolism and synthesis are modified, with metabolomic analysis isolating tryptophan metabolism as a primary altered pathway. As the field of metabolism is revisited by epilepsy researchers, and animal models are guided by precision medicine, the connections between redox processes and metabolism will be further illuminated.
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Robert, M. C., and O. Vidal. "Crystallization in Gels and Related Methods." In Crystallization of Nucleic Acids and Proteins. Oxford University Press, 1999. http://dx.doi.org/10.1093/oso/9780199636792.003.0010.

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From the first studies showing the feasibility of macromolecular crystal growth in gels (1), an increasing attention has been paid to applications of gel techniques to the domain of biological macromolecules. Confidence in these techniques is such that kits of crystallization in gels are now commercially available (Hampton Research, Laguna Hills, CA, USA). Basically, the protein crystallization process consists of two consecutive steps: • first, the transport of growth units towards the surface of the crystals • second, the incorporation of the growth units into a crystal surface position of high bond strength. The whole growth process is dominated by the slowest of these two steps and is either transport controlled or surface controlled. Avoiding convection in the growth environment will increase the possibility of growing the crystal under slow diffusive mass transport providing that the surface interaction kinetics are faster than the characteristic diffusive flow of macromolecules (in the range of 10-6 cm2/sec for proteins). The ratio between transport to surface kinetics, which can be tuned by either enhancing or reducing transport processes in the solution, has been shown (2) to control the amplitude of growth rate fluctuations (which is thought to reduce crystal quality). These are the main reasons why gels (as well as capillaries and microgravity conducted experiments), if correctly designed, are expected to enhance the quality of crystals. This quality enhancement (3), as well as the possibility of getting crystals when conventional solution techniques failed (4), have been experimentally demonstrated. However, up to now, gel methods have been used on a rather empirical basis, as a simple transposition of solution techniques, and recent fundamental studies of nucleation and growth in gels show that the situation is not as simple as first expected (5, 6). After summarizing the main characteristics of crystal growth in gels, we will examine what are the best conditions using a gel method. Recipes for the preparation of different gel growth experiments will be given. Considering gel growth as a possible simulation of experiments under reduced gravity, recent results of space experiments will be reviewed. Mention will also be made to growth under hypergravity conditions.
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Conference papers on the topic "Whey protein ratio"

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Kulikov, Denis, Ruzaliya Ulanova, and Valentina Kolpakova. "COMPREHENSIVE BIOTECHNOLOGICAL APPROACH TO PROCESSING OF PEA FLOUR FOR FOOD AND FODDER PURPOSES." In GEOLINKS Conference Proceedings. Saima Consult Ltd, 2021. http://dx.doi.org/10.32008/geolinks2021/b1/v3/06.

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Investigations were carried out to optimize the growth parameters of the symbiosis of cultures of the yeast Saccharomyces cerevisiae 121 and the fungus Geotrichum candidum 977 on whey waters formed from pea flour as a secondary product in the production of protein concentrates after precipitation of proteins at the isoelectric point. The whey remaining after protein precipitation is bioconverted at optimal parameters of crop growth (pH of the medium, amount of inoculum, temperature) with the formation of microbial plant concentrate (MPC) for feed purposes. Serum cultures assimilated stachyose, glucose, maltose, arabinose, and other pentoses. The mass fraction of protein in the concentrate was 57.90-61.68 % of DS. The composition of MPC obtained from biomass is balanced in essential amino acids with a speed of 107-226 %. The fatty acid composition is represented by 97 % fatty acids and 3 % - esters, aldehydes, ketones with the properties of fragrances, photo stabilizers, odor fixers, preservatives and other compounds. The ratio of the sum of saturated and unsaturated acids is 1:3, the content of cis-isomers is 91.1 %, trans-isomers are 5.1 %, omega-6 fatty acids are 19.73 %. The quality and safety indicators indicated that it is promising for use in the diet of animals.
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Yang, Jasmin, Fernanda Furlan Goncalves Dias, and Juliana M. Leite Nobrega De Moura Bell. "Sequential Fractionation as a Tool for Understanding the Physicochemical and Thermal Properties of Aqueous and Enzyme-assisted Aqueous Extracted Black Bean Proteins." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/qivq4253.

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Black bean proteins were sequentially extracted and characterized to understand the contribution of different protein classes to the physicochemical and thermal properties of black bean protein extracts produced with commercially-feasible extraction processes (i.e., aqueous extraction process, AEP, and enzyme-assisted aqueous extraction process, EAEP). The Osborne fractionation method was used to produce protein fractions rich in albumins (56%), globulins (22%), prolamins (0.65%), and glutelins (16%). AEP (pH 9.0, 50 °C, 1:10 solids-to-liquid ratio, 60 min) and EAEP (same conditions as AEP, except by the addition of 0.5% (w/w) alkaline protease) enabled the extraction of 75 and 81% of the bean flour protein, respectively. The protein molecular weight distribution showed that the AEP generates a mixture of albumins, globulins, and high-molecular weight glutelins while the EAEP hydrolyzed a majority of the ~42-48 kDa phaseolin into ~26.5 kDa fragments. EAEP proteins exhibited decreased surface hydrophobicity and increased absolute zeta potential values in relation to AEP proteins. The thermal stability of AEP and EAEP proteins decreased compared to that of the albumin- and globulin-rich fractions, likely due to partial denaturation in alkaline extraction conditions. However, the nearly identical thermal transition behavior of the AEP (To = 85.2 °C, Td = 92.0 °C) and EAEP (To = 84.1 °C, Td = 92.3 °C) proteins suggests that enzymatic hydrolysis did not significantly affect the thermal properties of bean proteins. Furthermore, the physicochemical modifications observed when enzymes were used during the extraction resulted in proteins with higher solubility at pH 4.0 (27% for AEP vs. 60% for EAEP). The results of this study demonstrate that aqueous extraction methods are effective in extracting albumins, globulins, and glutelins from black beans. Moreover, the use of commercial enzymes to assist protein extraction is a feasible method to improve bean protein extractability and functionality while retaining their thermal stability.
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Marcovina, S., R. Coppola, M. P. Protti, C. Gelfi, and P. M. Mannucci. "EDTA-DEPENDENT MONOCLONAL ANTIBODIES TO HUMAN PROTEIN S." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644294.

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Splenocytes from a Balb/c mouse immunized with purified human protein S (PS) were fused with murine hybridoma cell line SP2/0-Agl4 and cultured in Iscove's medium without addition of fetal bovine serum. Hybrid supernatants were screened for the presence of specific antibodies by solid-phase ELISA and cloned by the limiting dilution technique. Pour clones, named S2, S3, S8, and S10, were selected, recloned several times, and injected intraperitoneally into Balb/c mice for the production of antibody-rich ascitic fluid. The monoclonal antibodies (Mabs), all of IgGl subclass with k light chain, were purified from ascitic fluid by Protein-A chromatography. The specificity of Mabs was controlled by the immunoblotting technique: the Mabs appeared to react only with two plasma proteins, one with a MW of about 70.000 dal tons comigrating with purified PS, and the other with a MW >300.000 da that is likely to be the C4b-binding protein-PS complex. No interaction has been observed with PS-depleted plasma. As tested by a fluid phase radio immunoassay, the binding of Mabs to PS was significantly higher in the presence of EDTA while was totally inhibited in the presence of Ca2+. Scatchard plot analysis of the binding between 125I-PS and Mabs showed that the binding affinity of the antibodies ranged from 108 to 109 1/mol. Each EDTA-dependent Mab was then immobilized on Sepharose 4B-CNBr and used to purify PS from barium precipitation of citrated plasma. The fraction eluted with 2 mmol of CaCl2 from the immunoadsorbent appeared to contain only two proteins when stained with Cocmassie Blue. By immuno blotting, all Mabs reacted with both proteins, one comigrating with purified PS and the other with a MW >300.000. Essentially homogeneous PS, free from the high MW component, was obtained when the barium citrate adsorbate was applied to a DEAE-Sephadex column and the protein peack containing the balk of PS was sussequently applied to the immunoadsorbent and eluted with 2 mmol CaCl2.In summary, we have described an unusual set of EDTA-dependent monoclonal antibodies to PS and their use for the purification of homogeneous protein S from human plasma.
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Adams, G. A., and C. Hallée. "THROMBOSPONDIN ADSORPTION AND PLATELET ADHESION TO SURFACES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643589.

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Recent research into cell adhesion has focused on a tripeptide sequence arg-gly-asp (RGD) that is common to a number of cytoadhesive proteins such as von Willebrand factor, fibronectin and fibrinogen. We have previously reported that thrombospondin (TSP) inhibited platelet adhesion to RGD proteins. On further purification of TSP, the inhibitory activity separated away from the TSP. In this report, we demonstate that TSP adsorbs to surfaces and promotes platelet adhesion and thus may belong to this family of cytoadhesins. TSP was purified by heparin affinity chromatography, ammonium sulfate precipitation and sucrose gradient ultracentrifugation. Final preparations were free of TSP aggregates and gave one band on SDS-PAGE. Washed human platelets were radiolabelled, combined with red blood cells and perfused through protein-coated glass or polyethylene (PE) tubes for 7 mins. at a shear rate of 100 s™1. TSP supported platelet adhesion to the same level as fibrinogen (FG), but less than collagen. Platelets were spread but no thrombi were present on the TSP or FG-coated tubes while thrombi formed on collagen-coated tubes. Levels of adsorption were similar for purified solutions of radioiodinated FG or TSP on both glass and PE surfaces. The competitive interactions between these proteins during adsorption to surfaces indicated at equimolar amounts the TSP and FG both deposited on the surface but as FG:TSP ratio increased FG was preferentially adsorbed. These results indicate that TSP is a cytoadhesive protein for platelets when it is adsorbed to surfaces. Thus, the release of TSP from platelets may promote haemostasis or thrombogenesis.(supported by Ontario Heart Foundation, Canada)
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Peterson, C. B., C. M. Noyes, J. M. Pecon, F. C. Church, and M. N. Blackburn. "LYSINE-125 IS ESSENTIAL FOR HEPARIN BINDING TO ANTITHROMBIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643769.

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Identification of lysyl residue(s) in human plasma antithrombin required for binding of heparin was approached using chemical modification with the amino-group reagent, pyridoxal-5'-phosphate. Modification of antithrombin (AT) with limiting amounts of reagent yields an average incorporation of the phos-phopyridoxyl label into one lysine per protein molecule. Fractionation of the labeled AT by affinity chromatography on heparin-Sepharose separated a phosphopyridoxylated AT species devoid of heparin binding (Pool I) from modified protein which retained affinity for heparin (Pool II). Pool I contained an average of 1.6 mol phosphopyridoxyl label per mol AT, whereas Pool II was labeled to a lesser extent, with a ratio of 1.0 mol phosphopyridoxyl per mol protein. To generate peptide maps of the two AT species, the proteins were reductively denatured, S-carboxymethylated, and digested with trypsin. Fractionation of the tryptic digests by reverse-phase HPLC indicated one peak in the chromatogram of the non-heparin-binding species to be clearly different when compared to the chromatogram of the heparin-binding species. Upon sequencing of the unique peptide by automated Edman degradation, the modified residue was identified as Lys-125 in the primary sequence of AT. Additionally, AT was reacted with pyridoxal-5 ′-phosphate in the presence of added heparin for comparison with protein modified in the absence of heparin. Overall incorporation of the phosphopyridoxyl label was 3-4 mol reagent per mol protein, without inclusion of heparin during the modification reaction, and only 2-3 mol pyridoxyl per mol protein with heparin added. Tryptic peptide maps of these two modified ATs indicated that eight lysine residues are "protected" from modification by addition of heparin. The "protected" lysines identified, in addition to the essential Lys-125, are residues 11, 39, 133, 136, 257, 275, and 287. Identification of Lys-125 as the critical lysine for heparin binding strongly supports previous data which indicates that the heparin-binding domain of AT is located at the N-termi-nus within one of the disulfide cross-linked loops of the protein.
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Bibik, O. I., and E. A. Sumbaev. "HISTOCHEMICAL REACTIVITY OF THE PARENCHYMA AS CRITERION OF THE MECHANISM OF ANTIHELMINTIC ACTION ON THE HOMEOSTASIS OF THE PARASITE." In THEORY AND PRACTICE OF PARASITIC DISEASE CONTROL. All-Russian Scientific Research Institute for Fundamental and Applied Parasitology of Animals and Plant – a branch of the Federal State Budget Scientific Institution “Federal Scientific Centre VIEV”, 2023. http://dx.doi.org/10.31016/978-5-6048555-6-0.2023.24.90-94.

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Analysis of histologic specimens made from trematodes according to the generally accepted method before and after the action of anthelmintics and stained in a Schick test for the detection of glycogen, and with bromophenol blue for proteins, and toluidine blue for hexosaminoglycans using light microscopy showed that the action of the preparation in the body of trematodes caused metabolic disorders. After the action of anthelmintics, the histochemical reactivity of the connective tissue of trematodes, the parenchyma, changed. Tissue reaction to the dye increased, decreased or was absent. Weakened or disappeared metachromatic staining indicates a decrease in the amount of acid mucopolysaccharides. The Schick test demonstrates that after the action of the anthelmintic on the parasite, glycogen disappears, and the carbohydrate components are redistributed and quantitatively changed. A change in color when stained with bromophenol blue for proteins indicates a change in their nature and destruction. Histochemical analysis provides information on the quantitative and qualitative content of carbohydrate and protein compounds in the trematode parenchyma and objectively allows us to reveal the change in their ratio and nature after anthelmintics, and therefore to establish the mechanism and effect of drugs on the homeostatic disruption in the parasite's body after the host undergoes chemotherapy.
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Preissner, K. T., and P. Sie. "S PROTEIN/VITRONECTIN NEUTRALIZES THE ANTICOAGULANT ACTIVITY OF GLYCOSAMINOGLYCANS IN THE INHIBITION OF THROMBIN BY HEPARIN COFACTOR II." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643633.

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The complement inhibitor S protein, which is identical to the adhesive protein vitronectin, functions as heparin-neutralizing factor by protecting thrombin against fast inactivation by antithrombin III. The interference of S protein with glycos-aminoglycan-catalyzed inhibition of thrombin by heparin cofactor II was investigated in a purified system. In the presence of 0.3 μg/ml heparin, or 0.5 μg/ml pentosan polyphosphate (SP 54), or 2 μg/ml dermatan sulfate, S protein induced a concentration-dependent reduction of the inhibition rate of thrombin by heparin cofactor II. This resulted in a decrease of the apparent pseudo-first order rate constants by about 17-fold (heparin), or about 7-fold (SP 54), but only by about 2-fold for dermatan sulfate at a physiological ratio of S protein to heparin cofactor II. Likewise, S protein significantly counteracted the anticoagulant activity of heparin and SP 54 bot not of dermatan sulfate when tested in an inhibition assay using various concentrations of glycosaminoglycans. For heparin, the activity of S protein at the point of 50% inhibition of thrombin was expressed in the range 0.06-0.6 μg/ml (0.01-0.1 U/ml) and for SP 54 in the range 0.3-2 pg/ml. Exposure of the glycos-aminoglycan-binding region of S protein by reduction and carb-oxymethylation of the protein even increased the neutralizing activity of S protein towards heparin and SP 54. S protein not only was found together with thrombin in a binary complex. S protein also became incorporated into a ternary complex with thrombin and heparin cofactor II as judged by crossed immunoelectrophoresis, regardless whether complex formation was initiated by heparin or dermatan sulfate. These findings underline the role of S protein as potent glycosaminoglycan-neutral-izing protein in plasma and as scavenger protein which may bind to enzyme-inhibitor complexes of the coagulation system.
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Fang, Baochen, and Jiajia Rao. "Functional, nutritional properties and aroma profile of hemp protein isolate by reverse micelles extraction technique: impact of defatting processing." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/wzgi5968.

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There is an increased awareness of the incorporation of hemp protein in a commercial product on account of its high nutritional value and neutral flavor. One of the factors that impact the functional properties of hemp protein is the isolation conditions. In recent years, reverse micelles (RMs) has emerged as a powerful technique for extracting protein and enzyme because of low cost, convenience, and potential for scaling up in the manufacturing process. For oil crops, it generally requires long defatting processing before protein extraction. Therefore, it would be interesting to investigate whether the defatting of hempseed flour would impact on physicochemical properties of hemp protein using the RM extraction method. Our results revealed that high protein recovery yield (69.37-70.21%) and protein purity (92.76-95.2%) of hemp protein isolate (HPI) could be obtained through the RM technique using either non-defatted hemp flour (ND-HF) or defatted hemp flour (D-HF). Concerning the defatting processing, both HPIs showed great similarity in protein composition, and functional properties including solubility, thermal stability, foaming, and emulsifying properties. Interestingly, HPI obtained from ND-HF had higher essential amino acid ratio when compared to D-HF. Beyond that, distinct gelling behaviors (least gelling concentration, gel strength, and color) have been observed. The HPI gel obtained from ND-HF displayed a higher least gelling concentration (4%) with yellowish color than that of HPI gel from D-HF (2%). In terms of aroma profile, a significantly high number of aromatic compounds with a greater abundancy were detected in HPI from ND-HF (33) as compared to HPI isolated from D-HF (26), which contributed to the different process conditions and lipid content. The research findings provided an eco-friendly protein isolation method with premium functional attributes, especially for oil crops, which pave the way for the future application of RMs in a wide range of protein extraction.
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Kutuzova, Anel, Elena Provornaya, Ekaterina Sedova, and Nadezhda Tsybenko. "Feed quality when using new varieties of legume grass species in improved legume-cereals grass stands in cycles and years of use." In Multifunctional adaptive fodder production. ru: Federal Williams Research Center of Forage Production and Agroecology, 2022. http://dx.doi.org/10.33814/mak-2022-28-76-19-24.

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The article presents the results of studies of the quality of pasture feed in the dynamics on the cycles of use of legume-cereals grass stands, including new zoned varieties (creeping and meadow clover, alfalfa variable). Evaluation of the crude protein content of the feed revealed isolated cases (10–15% of the database) of a decrease in its concentration below the third class. Therefore, to guarantee the preservation of feed quality at the level of 1–3 classes, it is proposed to create 2–3 legume-cereals grass stands in the structure of the late link in different ratios of their area depending on the location and soil conditions.
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Chirico Scheele, Stefania, Mohammed Naimul Hoque, Gordon Christopher, and Paul F. Egan. "Printability and Fidelity of Protein-Enriched 3D Printed Foods: A Case Study Using Cricket and Pea Protein Powder." In ASME 2021 International Design Engineering Technical Conferences and Computers and Information in Engineering Conference. American Society of Mechanical Engineers, 2021. http://dx.doi.org/10.1115/detc2021-67783.

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Abstract 3D food printing has received high attention in personalized meal production and customized food designs in recent years due to its potential advantages over traditional food manufacturing methods. A current challenge in 3D food printing is the design of extrudable food materials that enable customized shape fabrication and retention. Additives such as starches and gums have been employed to improve food printability, however, these often detrimentally affect taste, texture, and nutrients. Our study explores the printability and shape fidelity of mashed potatoes when adding protein-rich cricket and pea protein powders. Different percentages of these additives (5%, 15%, and 30%) with varied water to protein ratios (0, 1, 2, and 3) were added to 100g of mashed potatoes. Mashed potatoes with the addition of cricket powder and pea powder provided the highest fidelity prints for water to additive ratios of 2 and 3, respectively. Rheological testing demonstrated these high-fidelity prints had complex modulus values ranging from 15Pa to 25Pa. Trade-offs were explored between print fidelity, complex modulus, and protein content for mashed potatoes with cricket protein that highlighted the relative trade-offs in 3D food printing recipes. These findings demonstrate that a design space including shape fidelity, printability, and nutritional profile provides rich trade-offs for promoting user satisfaction and health, thereby providing designers new opportunities to leverage 3D food printing to provide value for consumer needs and health.
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Reports on the topic "Whey protein ratio"

1

Guy, Charles, Gozal Ben-Hayyim, Gloria Moore, Doron Holland, and Yuval Eshdat. Common Mechanisms of Response to the Stresses of High Salinity and Low Temperature and Genetic Mapping of Stress Tolerance Loci in Citrus. United States Department of Agriculture, May 1995. http://dx.doi.org/10.32747/1995.7613013.bard.

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The objectives that were outlined in our original proposal have largely been achieved or will be so by the end of the project in February 1995 with one exception; that of mapping cold tolerance loci based on the segregation of tolerance in the BC1 progeny population. Briefly, our goals were to 1) construct a densely populated linkage map of the citrus genome: 2) map loci important in cold and/or salt stress tolerance; and 3) characterize the expression of genes responsive to cold land salt stress. As can be seen by the preceding listing of accomplishments, our original objectives A and B have been realized, objective C has been partially tested, objective D has been completed, and work on objectives E and F will be completed by the end of 1995. Although we have yet to map any loci that contribute to an ability of citrus to maintain growth when irrigated with saline water, our very encouraging results from the 1993 experiment provides us with considerable hope that 1994's much more comprehensive and better controlled experiment will yield the desired results once the data has been fully analyzed. Part of our optimism derives from the findings that loci for growth are closely linked with loci associated with foliar Cl- and Na+ accumulation patterns under non-salinization conditions. In the 1994 experiment, if ion exclusion or sequestration traits are segregating in the population, the experimental design will permit their resolution. Our fortunes with respect to cold tolerance is another situation. In three attempts to quantitatively characterize cold tolerance as an LT50, the results have been too variable and the incremental differences between sensitive and tolerant too small to use for mapping. To adequately determine the LT50 requires many plants, many more than we have been able to generate in the time and space available by making cuttings from small greenhouse-grown stock plants. As it has turned out, with citrus, to prepare enough plants needed to be successful in this objective would have required extensive facilities for both growing and testing hardiness which simply were not available at University of Florida. The large populations necessary to overcome the variability we encountered was unanticipated and unforeseeable at the project's outset. In spite of the setbacks, this project, when it is finally complete will be exceedingly successful. Listing of Accomplishments During the funded interval we have accomplished the following objectives: Developed a reasonably high density linkage map for citrus - mapped the loci for two cold responsive genes that were cloned from Poncirus - mapped the loci for csa, the salt responsive gene for glutathione peroxidase, and ccr a circadian rhythm gene from citrus - identified loci that confer parental derived specific DNA methylation patterns in the Citrus X Poncirus cross - mapped 5 loci that determine shoot vigor - mapped 2 loci that influence leaf Na+ accumulation patterns under non-saline conditions in the BC1 population - mapped 3 loci that influence leaf Na+ accumulation paterns during salt sress - mapped 2 loci that control leaf Cl- accumulation patterns under non-saline conditions - mapped a locus that controls leaf Cl- accumulation patterns during salt stress Screened the BC1 population for growth reduction during salinization (controls and salinized), and cold tolerance - determined population variation for shoot/root ratio of Na+ and Cl- - determined levels for 12 inorganic nutrient elements in an effort to examine the influence of salinization on ion content with emphasis on foliar responses - collected data on ion distribution to reveal patterns of exclusion/sequestration/ accumulation - analyzed relationships between ion content and growth Characterization of gene expression in response to salt or cold stress - cloned the gene for the salt responsive protein csa, identified it as glutathione peroxidase, determined the potential target substrate from enzymatic studies - cloned two other genes responsive to salt stress, one for the citrus homologue of a Lea5, and the other for an "oleosin" like gene - cold regulated (cor) genes belonging to five hybridization classes were isolated from Poncirus, two belonged to the group 2 Lea superfamily of stress proteins, the others show no significant homology to other known sequences - the expression of csa during cold acclimation was examined, and the expression of some of the cor genes were examined in response to salt stress - the influence of salinization on cold tolerance has been examined with seedling populations - conducted protein blot studies for expression of cold stress proteins during salt stress and vice versa
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2

Chejanovsky, Nor, and Suzanne M. Thiem. Isolation of Baculoviruses with Expanded Spectrum of Action against Lepidopteran Pests. United States Department of Agriculture, December 2002. http://dx.doi.org/10.32747/2002.7586457.bard.

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Our long-term goal is to learn to control (expand and restrict) the host range of baculoviruses. In this project our aim was to expand the host range of the prototype baculovirus Autographa cali/arnica nuclear polyhedrosis virus (AcMNPV) towards American and Israeli pests. To achieve this objective we studied AcMNPV infection in the non-permissive hosts L. dispar and s. littoralis (Ld652Y and SL2 cells, respectively) as a model system and the major barriers to viral replication. We isolated recombinant baculoviruses with expanded infectivity towards L. dispar and S. littoralis and tested their infectivity towards other Lepidopteran pests. The restricted host range displayed by baculoviruses constitutes an obstacle to their further implementation in the control of diverse Lepidopteran pests, increasing the development costs. Our work points out that cellular defenses are major role blocks to AcMNPV replication in non- and semi-permissive hosts. Therefore a major determinant ofbaculovirus host range is the ability of the virus to effectively counter cellular defenses of host cells. This is exemplified by our findings showing tliat expressing the viral gene Ldhrf-l overcomes global translation arrest in AcMNPV -infected Ld652Y cells. Our data suggests that Ld652Y cells have two anti-viral defense pathways, because they are subject to global translation arrest when infected with AcMNPV carrying a baculovirus apoptotic suppressor (e.g., wild type AcMNPV carryingp35, or recombinant AcMNPV carrying Opiap, Cpiap. or p49 genes) but apoptose when infected with AcMNPV-Iacking a functional apoptotic suppressor. We have yet to elucidate how hrf-l precludes the translation arrest mechanism(s) in AcMNPV-infected Ld652Y cells. Ribosomal profiles of AcMNPV infected Ld652Y cells suggested that translation initiation is a major control point, but we were unable to rule-out a contribution from a block in translation elongation. Phosphorylation of eIF-2a did not appear to playa role in AcMNPV -induced translation arrest. Mutagenesis studies ofhrf-l suggest that a highly acidic domain plays a role in precluding translation arrest. Our findings indicate that translation arrest may be linked to apoptosis either through common sensors of virus infection or as a consequence of late events in the virus life-cycle that occur only if apoptosis is suppressed. ~ AcMNPV replicates poorly in SL2 cells and induces apoptosis. Our studies in AcMNPV - infected SL2ceils led us to conclude that the steady-state levels of lEI (product of the iel gene, major AcMNPV -transactivator and multifunctional protein) relative to those of the immediate early viral protein lEO, playa critical role in regulating the viral infection. By increasing the IEl\IEO ratio we achieved AcMNPV replication in S. littoralis and we were able to isolate recombinant AcMNPV s that replicated efficiently in S. lifforalis cells and larvae. Our data that indicated that AcMNPV - infection may be regulated by an interaction between IE 1 and lED (of previously unknown function). Indeed, we showed that IE 1 associates with lED by using protein "pull down" and immunoprecipitation approaches High steady state levels of "functional" IE 1 resulted in increased expression of the apoptosis suppressor p35 facilitating AcMNPV -replication in SL2 cells. Finally, we determined that lED accelerates the viral infection in AcMNPV -permissive cells. Our results show that expressing viral genes that are able to overcome the insect-pest defense system enable to expand baculovirus host range. Scientifically, this project highlights the need to further study the anti-viral defenses of invertebrates not only to maximi~e the possibilities for manipulating baculovirus genomes, but to better understand the evolutionary underpinnings of the immune systems of vertebrates towards virus infection.
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3

Uni, Zehava, and Peter Ferket. Enhancement of development of broilers and poults by in ovo feeding. United States Department of Agriculture, May 2006. http://dx.doi.org/10.32747/2006.7695878.bard.

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The specific objectives of this research were the study of the physical and nutritional properties of the In Ovo Feeding (IOF) solution (i.e. theosmostic properties and the carbohydrate: protein ratio composition). Then, using the optimal solution for determining its effect on hatchability, early nutritional status and intestinal development of broilers and turkey during the last quarter of incubation through to 7 days post-hatch (i.e. pre-post hatch period) by using molecular, biochemical and histological tools. The objective for the last research phase was the determination of the effect of in ovo feeding on growth performance and economically valuable production traits of broiler and turkey flocks reared under practical commercial conditions. The few days before- and- after hatch is a critical period for the development and survival of commercial broilers and turkeys. During this period chicks make the metabolic and physiological transition from egg nutriture (i.e. yolk) to exogenous feed. Late-term embryos and hatchlings may suffer a low glycogen status, especially when oxygen availability to the embryo is limited by low egg conductance or poor incubator ventilation. Much of the glycogen reserve in the late-term chicken embryo is utilized for hatching. Subsequently, the chick must rebuild that glycogen reserve by gluconeogenesis from body protein (mostly from the breast muscle) to support post-hatch thermoregulation and survival until the chicks are able to consume and utilize dietary nutrients. Immediately post-hatch, the chick draws from its limited body reserves and undergoes rapid physical and functional development of the gastrointestinal tract (GIT) in order to digest feed and assimilate nutrients. Because the intestine is the nutrient primary supply organ, the sooner it achieves this functional capacity, the sooner the young bird can utilize dietary nutrients and efficiently grow at its genetic potential and resist infectious and metabolic disease. Feeding the embryo when they consume the amniotic fluid (IOF idea and method) showed accelerated enteric development and elevated capacity to digest nutrients. By injecting a feeding solution into the embryonic amnion, the embryo naturally consume supplemental nutrients orally before hatching. This stimulates intestinal development to start earlier as was exhibited by elevated gene expression of several functional genes (brush border enzymes an transporters , elvated surface area, elevated mucin production . Moreover, supplying supplemental nutrients at a critical developmental stage by this in ovo feeding technology improves the hatchling’s nutritional status. In comparison to controls, administration of 1 ml of in ovo feeding solution, containing dextrin, maltose, sucrose and amino acids, into the amnion of the broiler embryo increased dramatically total liver glycogen in broilers and in turkeys in the pre-hatch period. In addition, an elevated relative breast muscle size (% of broiler BW) was observed in IOF chicks to be 6.5% greater at hatch and 7 days post-hatch in comparison to controls. Experiment have shown that IOF broilers and turkeys increased hatchling weights by 3% to 7% (P<0.05) over non injected controls. These responses depend upon the strain, the breeder hen age and in ovo feed composition. The weight advantage observed during the first week after hatch was found to be sustained at least through 35 days of age. Currently, research is done in order to adopt the knowledge for commercial practice.
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4

Meidan, Rina, and Robert Milvae. Regulation of Bovine Corpus Luteum Function. United States Department of Agriculture, March 1995. http://dx.doi.org/10.32747/1995.7604935.bard.

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The main goal of this research plan was to elucidate regulatory mechanisms controlling the development, function of the bovine corpus luteum (CL). The CL contains two different sterodigenic cell types and therefore it was necessary to obtain pure cell population. A system was developed in which granulosa and theca interna cells, isolated from a preovulatory follicle, acquired characteristics typical of large (LL) and small (SL) luteal cells, respectively, as judged by several biochemical and morphological criteria. Experiments were conducted to determine the effects of granulosa cells removal on subsequent CL function, the results obtained support the concept that granulosa cells make a substaintial contribution to the output of progesterone by the cyclic CL but may have a limited role in determining the functional lifespan of the CL. This experimental model was also used to better understand the contribution of follicular granulosa cells to subsequent luteal SCC mRNA expression. The mitochondrial cytochrome side-chain cleavage enzyme (SCC), which converts cholesterol to pregnenolone, is the first and rate-limiting enzyme of the steroidogenic pathway. Experiments were conducted to characterize the gene expression of P450scc in bovine CL. Levels of P450scc mRNA were higher during mid-luteal phase than in either the early or late luteal phases. PGF 2a injection decreased luteal P450scc mRNA in a time-dependent manner; levels were significantly reduced by 2h after treatment. CLs obtained from heifers on day 8 of the estrous cycle which had granulosa cells removed had a 45% reduction in the levels of mRNA for SCC enzymes as well as a 78% reduction in the numbers of LL cells. To characterize SCC expression in each steroidogenic cell type we utilized pure cell populations. Upon luteinization, LL expressed 2-3 fold higher amounts of both SCC enzymes mRNAs than SL. Moreover, eight days after stimulant removal, LL retained their P4 production capacity, expressed P450scc mRNA and contained this protein. In our attempts to establish the in vitro luteinization model, we had to select the prevulatory and pre-gonadotropin surge follicles. The ratio of estradiol:P4 which is often used was unreliable since P4 levels are high in atretic follicles and also in preovulatory post-gonadotropin follicles. We have therefore examined whether oxytocin (OT) levels in follicular fluids could enhance our ability to correctly and easily define follicular status. Based on E2 and OT concentrations in follicular fluids we could more accurately identify follicles that are preovulatory and post gonadotropin surge. Next we studied OT biosynthesis in granulosa cells, cells which were incubated with forskolin contained stores of the precursor indicating that forskolin (which mimics gonadotropin action) is an effective stimulator of OT biosynthesis and release. While studying in vitro luteinization, we noticed that IGF-I induced effects were not identical to those induced by insulin despite the fact that megadoses of insulin were used. This was the first indication that the cells may secrete IGF binding protein(s) which regonize IGFs and not insulin. In a detailed study involving several techniques, we characterized the species of IGF binding proteins secreted by luteal cells. The effects of exogenous polyunsaturated fatty acids and arachidonic acid on the production of P4 and prostanoids by dispersed bovine luteal cells was examined. The addition of eicosapentaenoic acid and arachidonic acid resulted in a dose-dependent reduction in basal and LH-stimulated biosynthesis of P4 and PGI2 and an increase in production of PGF 2a and 5-HETE production. Indomethacin, an inhibitor of arachidonic acid metabolism via the production of 5-HETE was unaffected. Results of these experiments suggest that the inhibitory effect of arachidonic acid on the biosynthesis of luteal P4 is due to either a direct action of arachidonic acid, or its conversion to 5-HETE via the lipoxgenase pathway of metabolism. The detailed and important information gained by the two labs elucidated the mode of action of factors crucially important to the function of the bovine CL. The data indicate that follicular granulosa cells make a major contribution to numbers of large luteal cells, OT and basal P4 production, as well as the content of cytochrome P450 scc. Granulosa-derived large luteal cells have distinct features: when luteinized, the cell no longer possesses LH receptors, its cAMP response is diminished yet P4 synthesis is sustained. This may imply that maintenance of P4 (even in the absence of a Luteotropic signal) during critical periods such as pregnancy recognition, is dependent on the proper luteinization and function of the large luteal cell.
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