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Auswahl der wissenschaftlichen Literatur zum Thema „Bovine hemoglobin“
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Zeitschriftenartikel zum Thema "Bovine hemoglobin"
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Jordan, Shane D., und Earnest Alexander. „Bovine Hemoglobin“. Journal of Pharmacy Practice 26, Nr. 3 (06.08.2012): 257–60. http://dx.doi.org/10.1177/0897190012451928.
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Introduction: Management of severe symptomatic anemia in critically ill Jehovah’s Witness patients remains a challenge. The paucity of therapeutic alternatives to human red blood cells has prompted the use of blood substitutes. Case Report: A 19-year-old female Jehovah’s Witness patient presented to the emergency department following several episodes of syncope. She was found to have a positive Coombs test and was diagnosed with warm-bodied autoimmune hemolytic anemia. Upon admission, her hemoglobin was 8.4 g/dL, then dropped to a nadir of 2.8 g/dL 4 days later. She received traditional management with corticosteroids, intravenous immune globulin, rituximab, and partial splenic artery embolization. Despite these therapies, hemoglobin levels failed to respond, and she experienced signs of marked ischemia. A decision was made to give 2 units of Hemopure, a bovine hemoglobin-based oxygen carrier, and the hemoglobin levels increased to 8.7 g/dL 10 days later. The patient’s overall clinical condition improved leading to subsequent hospital discharge. Conclusion: This case exemplifies the ingenuity that health care practitioners must use in critical situations involving the medical management of anemic Jehovah’s Witness patients who refuse blood products. Hemopure was used as “bridging treatment” to help save a patient from the devastating effects of ischemia resulting from severe anemia.
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MATCHAM, G. W. J., J. M. CHAPSAL und D. GUILLOCHON. „Catalytic Activities of Bovine Hemoglobin“. Annals of the New York Academy of Sciences 501, Nr. 1 Enzyme Engine (Juni 1987): 21–35. http://dx.doi.org/10.1111/j.1749-6632.1987.tb45680.x.
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BRAEND, M., G. EFREMOV und A. RAASTAD. „GENETICS OF BOVINE HEMOGLOBIN D“. Hereditas 54, Nr. 3 (02.09.2009): 255–59. http://dx.doi.org/10.1111/j.1601-5223.1966.tb02020.x.
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Lima, Maria Celiana P., und Cristina T. Andrade. „Stroma-Free Hemoglobin from Bovine Blood“. Artificial Cells, Blood Substitutes, and Biotechnology 35, Nr. 4 (Januar 2007): 431–47. http://dx.doi.org/10.1080/10731190701460333.
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Shirahama, Hiroyuki, Koji Suzuki und Toshiro Suzawa. „Bovine hemoglobin adsorption onto polymer latices“. Journal of Colloid and Interface Science 129, Nr. 2 (Mai 1989): 483–90. http://dx.doi.org/10.1016/0021-9797(89)90462-1.
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Clementi, Maria E., Roberto Scatena, Alvaro Mordente, Saverio G. Condò, Massimo Castagnola und Bruno Giardina. „Oxygen Transport by Fetal Bovine Hemoglobin“. Journal of Molecular Biology 255, Nr. 1 (Januar 1996): 229–34. http://dx.doi.org/10.1006/jmbi.1996.0019.
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Goldman, Daniel W., Richard J. Breyer, David Yeh, Beth A. Brockner-Ryan und Abdu I. Alayash. „Acellular hemoglobin-mediated oxidative stress toward endothelium: a role for ferryl iron“. American Journal of Physiology-Heart and Circulatory Physiology 275, Nr. 3 (01.09.1998): H1046—H1053. http://dx.doi.org/10.1152/ajpheart.1998.275.3.h1046.
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We tested the hypothesis that chemical modifications used to produce stable, oxygen-carrying, Hb-based blood substitutes can induce cytotoxicity in endothelial cells in culture because of altered redox activity. We examined the interaction of hydrogen peroxide with nonmodified hemoglobin (HbA0) and two chemically modified hemoglobins, α-cross-linked hemoglobin (α-DBBF) and its polymerized form (poly-α-DBBF). Hydrogen peroxide-induced cell death (as assessed by lactate dehydrogenase release) in bovine aortic endothelial cells (BAEC) was completely inhibited by all three hemoglobin preparations, consistent with their known pseudoperoxidase activity [hemoglobin consumes peroxide as it cycles between ferric (Fe3+) and ferryl (Fe4+) hemes]. However, reaction of the modified hemoglobins, but not HbA0, with hydrogen peroxide induced apoptotic cell death (as assessed by morphological changes and DNA fragmentation) that correlated with the formation of a long-lived ferrylhemoglobin. A preparation of ferryl-α-DBBF free of residual peroxide rapidly induced morphological changes and DNA fragmentation in BAEC, indicative of apoptotic cell death. Redox cycling of chemically modified hemoglobins by peroxide yielded a persistent ferryl iron that was cytotoxic to endothelial cells.
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Wang, Ying, Linli Wang, Weili Yu, Dawei Gao, Guoxing You, Penglong Li, Shan Zhang et al. „A PEGylated bovine hemoglobin as a potent hemoglobin-based oxygen carrier“. Biotechnology Progress 33, Nr. 1 (31.10.2016): 252–60. http://dx.doi.org/10.1002/btpr.2380.
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D'Agnillo, Felice. „Redox active hemoglobin enhances lipopolysaccharide-induced injury to cultured bovine endothelial cells“. American Journal of Physiology-Heart and Circulatory Physiology 287, Nr. 4 (Oktober 2004): H1875—H1882. http://dx.doi.org/10.1152/ajpheart.00164.2004.
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The interaction of cell-free hemoglobin with lipopolysaccharide (LPS) is thought to aggravate the pathophysiology of sepsis and/or septic shock. This study examines the possible modulatory role of cell-free hemoglobin on LPS-induced apoptosis of cultured bovine aortic endothelial cells. Experiments were performed with or without fetal bovine serum, a source of LPS-binding protein and soluble CD14. In the absence of serum, LPS alone or coincubated with purified bovine hemoglobin (BvHb), human hemoglobin (Hb), or α-cross-linked Hb (ααHb) did not induce apoptosis. In the presence of serum, LPS induced significant apoptosis. LPS combined with BvHb, Hb, or ααHb produced the same extent of apoptosis as LPS alone. To examine whether the H2O2-driven redox activity of hemoglobin alters LPS-induced apoptosis, glucose oxidase was added to the system to generate a subtoxic flux of H2O2. The combined treatment of LPS, glucose oxidase, and BvHb, Hb, or ααHb enhanced apoptosis compared with LPS alone. These findings support a possible mechanism whereby the redox cycling of hemoglobin, and not its direct interaction with LPS, contributes to the hemoglobin-mediated enhancement of LPS-related pathophysiology.
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Marta, Maurizio, Maria Patamia, Alessandro Lupi, Mirca Antenucci, Mario Di Iorio, Sergio Romeo, Raffaele Petruzzelli, Massimo Pomponi und Bruno Giardina. „Bovine Hemoglobin Cross-Linked through the Chains“. Journal of Biological Chemistry 271, Nr. 13 (29.03.1996): 7473–78. http://dx.doi.org/10.1074/jbc.271.13.7473.
Der volle Inhalt der QuelleDissertationen zum Thema "Bovine hemoglobin"
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Komninou, Eliza Rossi. „Contribuição ao estudo da hematologia de bezerros da raça nelore, originados por meio da técnica de transferência nuclear de célula somática (TNCS) - Clonagem“. Universidade de São Paulo, 2008. http://www.teses.usp.br/teses/disponiveis/10/10136/tde-11082009-101644/.
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A presente pesquisa teve a finalidade de estudar a hematologia de bezerros clonados da raça Nelore, originados por meio da técnica de transferência nuclear de células somáticas (TNCS) por meio da avaliação do quadro eritrocitário, da dinâmica dos tipos de hemoglobina e do metabolismo do ferro destes animais durante o primeiro mês de vida. O delineamento experimental envolveu a colheita de 260 amostras de sangue e soro sanguíneo de 20 bezerros distribuídas nos seguintes momentos: imediatamente após o nascimento, 12 horas após o nascimento, 1 dia de vida, 2 , 3 , 4, 5, 7, 10, 15, 20 e 30 dias de vida. Os animais foram divididos em quatro grupos experimentais: 12 bezerros obtidos por meio da técnica de TNCS pelos laboratórios A e 8, 4 por meio de fertilização in vitro (FIV) e 4 por monta natural (MN). A ocorrência de anemia de grau moderado a grave, do tipo normocítico e normocrômico, foi observada em 100 % (5/5) dos 5 bezerros clonados pelo Laboratório A, enquanto a incidência nos bezerros clonados pelo Laboratório B foi igual a 14,2 % (1/7), nos bezerros obtidos por fertilização in vitro foi igual 50,0 % (2/4) e em bezerros obtidos por monta natural foi igual a 50,0 % (2/4). A avaliação do eritrograma dos bezerros cio nados pelo Laboratório A evidenciou que a anemia instalou-se gradualmente a partir das 12 horas de vida atingindo ao final da primeira semana, a, sua intensidade máxima, sendo observada a recuperação gradativa dos valores eritrograma a partir do 15°dia de vida. Os valores médios obtidos para o eritrograma dos bezerros clonados do Laboratório A no 7º dia de vida foram os seguintes: Hemácias - 4,33X106/mm3-; Volume Globular - 23 %, Taxa de Hemoglobina - 7,25 g/dL; VCM - 52,89 µ3-; HCM - 16,65 pg; CHCM - 31,47%. A anemia observada nos bezerros clonados pelo Laboratório A era de origem ferropriva, pois se evidenciou nesses animais uma significativa diminuição dos teores séricos de ferro associada à diminuição do índice de saturação da transferrina (1ST), enquanto os valores da capacidade total de ligação do ferro (CTLF) não sofreram influência durante o período. Os valores médios obtidos para o metabolismo de ferro dos bezerros clonados pelo Laboratório A no 7º dia de vida foram os seguintes: teores séricos de ferro - 47,35 mg/dL; capacidade total de ligação de ferro - 455,90 mg/dL, índice de saturação da transferrina - 9,64%. Durante o estudo dos tipos de hemoglobinas, utilizando-se técnica de eletroforese foram identificados três fenótipos de hemoblogina adulta (Hb-A; Hb-B e Hb-AB) e a presença de hemoglobina fetal (Hb-F), não sendo observadas anomalias que pudessem sugerir a ocorrência de hemoglobinopatias hereditárias e/ ou congênitas. Verificou-se que as taxas de Hb-A, nos clones com fenótipo Hb-AB e Hb-A, permaneceram estáveis durante todo o período experimental, enquanto nos bezerros obtidos por fertilização in vitro ou monta natural com os mesmos fenótipos (Hb-A e Hb-AB) observou-se a partir de 120 horas de vida um gradativo aumento das taxas de Hb-A. Durante a avaliação da dinâmica da hemoglobina do tipo fetal (Hb-F) no primeiro mês de vida observou-se, que todos os grupos animais apresentaram comportamento similar, caracterizado por sua diminuição com o desenvolvimento etário.The present work aimed to study the hematology of cloned Nelore calves produced using the technique of somatic cell nuclear transfer (SCNT), by evaluating erythrocyte parameters, hemoglobin dynamics, and iron metabolism in the animals during the first month after birth. The experimental design included the collection of 260 blood and blood serum samples from 20 calves in the following times: immediately after birth, 12 hours after birth, 1st of life, 2nd, 3rd, 4th, 5th, 7th, 20th and 30th day of life. The animals were classified in four experimental groups: 12 calves produced, using SCNT for two commercial laboratories (laboratory A=5 calves and laboratory B= 7 calves), four calves produced by in vitro fertilization (IVF) and four calves produced by natural mating (NM). Mild to severe normocytic and normochromic anemia was observed in 100% (5/5) cloned calves from laboratory A, and 14.2% (117) cloned calves from laboratory B. In both IVF and NM calves, anemia was observed in 50% (214) of the calves. Erytrogram evaluation of cloned calves from laboratory A showed that anemia developed gradually from 12 hours after birth, was most intense at the end of the first week, and then erytrogram normal values were recovered after the 15th day of life. Mean values for the laboratory A cloned calves erytrogram in the 7th day of life were the following: Red cells 4033X106/mm3, hematocrit 23%, hemoglobin 7.25g/dL, MCV 52.89µ3-; MCH 16.65, MCHC 31.47%. Anemia observed in cloned calves from laboratory A was caused by iron deficiency, since a significant decrease in iron se rum levels together with a decrease in transferrin saturation index (TSI) was confirmed. At the same time, Total iron-binding capacity (TIBC) was not changed in this period of time. Mean iron metabolism values for cloned calves from laboratory A were the following: serum iron amount: 47,35mg/dL, TIBC 455,90 mg/dL and TSI 9,64%. Hemoglobin identification by eletrophoresis identified three adult hemolglobin phenotypes (A-Hb; B-Hb e AB-Hb) and the fetal hemoglobin (F-HB), and there was no sign of hereditary hemoglobin disorders were observed. The rate of A-Hb in cloned calves with A-Hb and AB-Hb phenotypes was maintained during the experimental period. Nonetheless, for the IVF calves with the same phenotypes (A-Hb and AB-Hb) a constant increase in the A-Hb was noticed. For the evaluation of F-Hb dynamics in the first month of life, results showed similar pattern, characterized by its decrease with age.
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Zhou, Yipin. „Synthesis and Biophysical Characterization of Polymerized Hemoglobin Dispersions of Varying Size and Oxygen Affinity as Potential Oxygen Carriers for use in Transfusion Medicine“. The Ohio State University, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=osu1321406529.
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Outman, Ahlam. „Production de peptides anticancéreux à partir des hydrolysats d'hémoglobine humaine et bovine, avec des propriétés additionnelles antibactériennes et antioxydantes“. Electronic Thesis or Diss., Université de Lille (2022-....), 2023. http://www.theses.fr/2023ULILR082.
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L'hémoglobine, la protéine prédominante dans le cruor, responsable de la couleur rouge du sang chez les mammifères, est reconnue pour être une source riche en peptides bioactifs après hydrolyse par la pepsine porcine. Ces peptides sont principalement connus pour leurs propriétés antimicrobiennes. Cependant, ces derniers se démarquent par leur capacité à cibler spécifiquement les cellules cancéreuses tout en préservant les cellules saines à prolifération rapide. Cette thèse vise à élaborer une stratégie de valorisation de l'hémoglobine humaine et bovine, en produisant des peptides bioactifs, puis en explorant leur potentiel dans la lutte contre le cancer, tout en évaluant leurs propriétés anticancéreuses, antibactériennes et antioxydantes.Dans ce travail, le potentiel de l'hémoglobine humaine à contenir des peptides bioactifs a d'abord été étudié in silico en comparaison avec l'hémoglobine bovine à l'aide d'outils bioinformatiques. Les résultats de blast ont montré une identité élevée, 88% et 85% respectivement, indiquant une forte similarité entre les chaînes α et β. Les conditions d'hydrolyse enzymatique (23°C, E/S = 1/11, pH 3,5) ont été validé sur l'hémoglobine humaine et a permis une production efficace du peptide α137-141. En effet, plus de 60% de la production totale de peptides α137-141 est obtenue en seulement 30 minutes d'hydrolyse, atteignant un pic de production à 3 h. De plus, le mécanisme d'hydrolyse enzymatique de ces deux types d'hémoglobine suit un schéma similaire, selon un mécanisme zipper.L'hydrolyse enzymatique a également été réalisée à hautes concentrations en hémoglobine (1, 2, 8 et 10%, p/v), permettant de produire l'α137-141 à grande échelle.Ensuite, les résultats ont montré une forte activité antimicrobienne des hydrolysats peptidiques contre six souches bactériennes, indépendamment du niveau de concentration initiale du substrat. Les hydrolysats ont également montré une forte activité antioxydante, mesurée par quatre tests différents. De plus, les activités antimicrobiennes et antioxydantes des hydrolysats d'hémoglobine humaine et bovine ont montré peu ou pas de différence significative, seul le niveau de concentration étant le facteur déterminant de leur activité.Le potentiel anticancéreux des peptides bioactifs issus de l'hydrolyse enzymatique de l'hémoglobine a été étudié. Les résultats obtenus à travers deux approches distinctes ont mis en lumière leur potentiel prometteur en tant qu'agents anticancéreux. L'investigation de paramètres clés tels que la concentration initiale d'hémoglobine, le degré d'hydrolyse et les caractéristiques structurales des peptides antimicrobiens avait mis en évidence l'influence de ces facteurs sur l'activité antimitotique des peptides. Le peptide α137-141 se distingue par une forte inhibition de la croissance des radicelles, avec des valeurs d'IC50 exceptionnellement basses, soit 10 à 15 fois supérieures à d'autres fractions, attribuées à son fort potentiel antimicrobien. Les analyses in vitro ont renforcé l'hypothèse selon laquelle l'inhibition de la synthèse protéique joue un rôle essentiel dans le mécanisme anticancéreux de ces peptides.Enfin, les résultats de l'étude par spectrométrie de masse ont montré la présence d'un certain nombre de peptides bioactifs, dont la majorité présente des caractéristiques similaires à celles mentionnées dans la littérature. De nouveaux peptides bioactifs ont également été identifiés dans l'hémoglobine humaine, tels que les peptides antibactériens PTTKTYFPHF (α37-46), FPTTKTYFPH (α36-45), TSKYR (α137-141) et STVLTSKYR (α133-141), ainsi que l'antioxydant TSKYR (α137-141) dont trois autres peptides opioïdes, un inhibiteur de l'ECA, un agent anticancéreux. Cette thèse offre une nouvelle approche innovante, combinant des propriétés antimicrobiennes, antioxydantes et anticancéreuses, ouvrant la voie à des traitements plus efficaces et moins nocifs pour les patientsHemoglobin, the predominant protein in cruor responsible for the red colour of mammalian blood, is known to be a rich source of bioactive peptides after hydrolysis by porcine pepsin. These peptides are mainly known for their antimicrobial properties. However, these peptides stand out for their ability to specifically target cancer cells while preserving rapidly proliferating healthy cells. The aim of this thesis is to develop a strategy for adding value to human and bovine haemoglobin by producing bioactive peptides and then exploring their potential in the fight against cancer, while assessing their anti-cancer, anti-bacterial and antioxidant properties.In this work, the potential of human hemoglobin to contain bioactive peptides was first studied in silico in comparison with bovine hemoglobin using bioinformatics tools. Blast results showed high identity, 88% and 85% respectively, indicating high similarity between α and β chains. The enzymatic hydrolysis conditions (23°C, E/S = 1/11, pH 3.5) were validated on human hemoglobin and enabled efficient production of the α137-141 peptide. Indeed, more than 60% of the total α137-141 peptide production was obtained in just 30 minutes of hydrolysis, reaching a production peak at 3 h. Furthermore, the mechanism of enzymatic hydrolysis of these two types of haemoglobin follows a similar pattern, according to a zipper mechanism. Enzymatic hydrolysis was also performed at high haemoglobin concentrations (1, 2, 8 and 10%, w/v), enabling large-scale production of α137-141.Next, the results showed strong antimicrobial activity of the peptide hydrolysates against six bacterial strains, independent of the initial substrate concentration level. The hydrolysates also showed strong antioxidant activity, measured by four different tests. In addition, the antimicrobial and antioxidant activities of the human and bovine haemoglobin hydrolysates showed little or no significant difference, with only the concentration level being the determining factor in their activity.The anticancer potential of bioactive peptides derived from the enzymatic hydrolysis of haemoglobin was studied. The results obtained using two distinct approaches highlighted their promising potential as anti-cancer agents. The investigation of key parameters such as the initial concentration of haemoglobin, the degree of hydrolysis and the structural characteristics of the antimicrobial peptides highlighted the influence of these factors on the antimitotic activity of the peptides. The α137-141 peptide stood out for its strong inhibition of rootlet growth, with exceptionally low IC50 values, 10 to 15 times higher than other fractions, attributed to its strong antimicrobial potential. In vitro analyses reinforced the hypothesis that inhibition of protein synthesis plays an essential role in the anti-cancer mechanism of these peptides.Finally, the results of the mass spectrometry study showed the presence of a number of bioactive peptides, the majority of which have characteristics similar to those reported in the literature. New bioactive peptides were also identified in human hemoglobin, such as the antibacterial peptides PTTKTYFPHF (α37-46), FPTTKTYFPH (α36-45), TSKYR (α137-141) and STVLTSKYR (α133-141), as well as the antioxidant TSKYR. (α137-141) including three other opioid peptides, an ACE inhibitor, an anticancer agent. This thesis offers a new innovative approach, combining antimicrobial, antioxidant and anticancer properties, paving the way for more effective and less harmful treatments for patients
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Estrela, Andreia Bergamo. „Degradação de vitelina e hemoglobina no carrapato bovino Rhipicephalus (Boophilus) microplus“. reponame:Biblioteca Digital de Teses e Dissertações da UFRGS, 2008. http://hdl.handle.net/10183/26613.
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O presente trabalho caracterizou alguns aspectos enzimáticos da digestão de vitelina e de hemoglobina no carrapato bovino Rhipicephalus (Boophilus) microplus. Um novo protocolo foi desenvolvido para a purificação de uma cisteíno endopeptidase de larvas do carrapato (R. microplus Larval Cysteine Endopeptidase; RmLCE). A seqüência parcial de aminoácidos de RmLCE mostrou similaridade com outra cisteíno endopeptidase descrita neste organismo (Boophilus microplus Cathepsin -L1; BmCL1). Vitelina (Vt), preparada a partir de homogenatos de ovos e larvas de R. microplus, foi degradada diferencialmente por RmLCE e VTDCE (Vitellin-Degrading Cysteine Endopeptidase; uma enzima de atividade semelhante purificada de ovos de R. microplus). RmLCE também apresentou capacidade de degradação de hemoglobina em pH 4,0, e a presença de uma atividade cisteíno endopeptidásica acídica em intestino de larvas foi demonstrada. A atividade peptidásica total, presente em homogenatos de ovos, larvas e intestino de partenóginas, sobre substrato sintético em pH 4,0, mostrou-se diferencialmente susceptível a inibidores de cisteíno e aspártico endopeptidases (E-64 e pepstatina A, respectivamente). A ação combinada dos dois inibidores inibiu completamente a atividade peptidásica. Estes inibidores também afetaram a degradação de vitelina e hemoglobina por homogenatos de larvas e intestino de partenóginas. A presença de pepstatina A inibiu cerca de 50 % da atividade sobre hemoglobina em larvas, enquanto E-64 foi capaz de inibir completamente a degradação das proteínas por ambos os homogenatos. Um enzima com atividade aspártico endopeptidásica presente em larvas de R. microplus foi parcialmente purificada e identificada por Western blot e seqüenciamento N-terminal como Boophilus Yolk Cathepsin (BYC). Esta enzima foi eluída de uma coluna de gel-filtração em pH ácido associada a uma atividade cisteíno endopeptidásica. A degradação de hemoglobina de forma sinérgica pela aspártico endopeptidase (BYC) e a cisteíno endopeptidase (RmLCE) purificadas de larva indica a existência de uma cascata enzimática responsável pela digestão de hemoglobina. Estes resultados sugerem que RmLCE tem um papel continuo na digestão de vitelina e hemoglobina durante o desenvolvimento de R. microplus.
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Ricardi, Evandro dos Santos [UNESP]. „Glutationa como agente alostérico em hemoglobina bovina, humana e de e matrinxã“. Universidade Estadual Paulista (UNESP), 2008. http://hdl.handle.net/11449/99652.
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ricardi_es_me_sjrp.pdf: 2273724 bytes, checksum: eed74e01870d5b90b7fb020a587b9ac0 (MD5)A Glutationa (GSH) é um tripeptídeo presente nas células, que em sua forma reduzida age como antioxidante, mantendo os grupamentos tiólicos nas proteínas em estado reduzido. Ao exercer função protetora, a glutationa é oxidada para sua forma dissulfeto, expondo quatro cargas negativas. A glutationa oxidada (GSSG) poderia interagir não covalentemente com moléculas capazes de ligar ânions, como a hemoglobina. Essa condição nos levou a investigar as possíveis mudanças estruturais e funcionais das hemoglobinas bovina, humana e majoritária do peixe matrinxã (Brycon cephalus) quando interagem alostericamente com a glutationa. As amostras de sangue bovina e humana foram purificadas e submetidas à eletroforese para verificação de pureza. As propriedades de ligação com oxigênio e controle alostérico foram analisados por tonometria a 20°C, calculando a afinidade de ligação com o O2 e a cooperatividade (n50). As condições experimentais adotadas foram, stripped, cloreto e glutationa oxidada (GSSG), nessas condições, as hemoglobinas bovina e humana apresentaram efeito Bohr alcalino. O cloreto induziu o maior efeito de diminuição da afinidade em praticamente todas as condições. As hemoglobinas apresentaram processo cooperativo de ligação de oxigênio, em todas as condições e em toda faixa de pH. No caso da hemoglobina bovina adulta, a GSSG aumentou a afinidade por O2, em toda a faixa de pH testada, enquanto para a humana isso ocorreu abaixo de pH 7,0. O cloreto capaz de diminuir a afinidade de forma efetiva em todas as condições. A hemoglobina bovina apresentou uma menor afinidade de ligação ao oxigênio em relação à hemoglobina humana. A glutationa oxidada atuou como efetor alostérico heterotrópico em hemoglobinas humana, bovina e matrinxã (Hb-II), aumentando a afinidade de ligação por oxigênio da hemoglobina. Entretanto, a glutationa na forma reduzida...
Glutathione (GSH) is an intracellular tripeptide, which in its reduced form acts as an antioxidant, keeping the cysteines in the reduced state. When exerting protective function, glutathione is oxidized to form its disulfide, exposing four negative charges. The oxidized glutathione (GSSG) could interact with molecules covalently able to bind anions, such as hemoglobin. That motivated us to investigate the possible structural and functional changes of bovine, human and a fish hemoglobin from the fish ‘matrinxã’ (Brycon cephalus) when they interact allosterically with glutathione. Samples of human and cattle blood were purified and subject to electrophoresis to verify their purity. The functional properties of oxygen binding and allosteric control were analyzed by the tonometric method at 20°C, calculating the affinity of O2-binding and cooperativity (n50). The tested experimental conditions involved hemoglobin in the absence (stripped) and in the presence of chloride and oxidized glutathione (GSSG). Under those circumstances, the human and bovine hemoglobins displayed an alkaline Bohr effect. Chloride induced the greatest effect of reducing affinity in all conditions. For all the experimental sets oxygen binding was cooperative. For bovine adult hemoglobin GSSG increased O2-affinity for all the tested pH values, whereas it occurred for human Hb for pH values above 7.0. Bovine Hb displayed lower O2-affinity than its human counterpart. Oxidized glutahione acted as a heterotropic allosteric effector in all the tested hemoglobins, increasing O2-affinity. However, GSH decreased O2-affinity of human and bovine Hbs. We assume that there is a binding site for GSSG at the R state, increasing O2-affinity, and another one for GSH at the T state, stabilizing its conformation and therefore lowering O2-affinity.
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Ricardi, Evandro dos Santos. „Glutationa como agente alostérico em hemoglobina bovina, humana e de e matrinxã /“. São José do Rio Preto : [s.n.], 2008. http://hdl.handle.net/11449/99652.
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Orientador: Gustavo Orlando Bonilla RodriguezBanca: Patrícia Caetano de Souza
Banca: Luiz Henrique Florindo
Resumo: A Glutationa (GSH) é um tripeptídeo presente nas células, que em sua forma reduzida age como antioxidante, mantendo os grupamentos tiólicos nas proteínas em estado reduzido. Ao exercer função protetora, a glutationa é oxidada para sua forma dissulfeto, expondo quatro cargas negativas. A glutationa oxidada (GSSG) poderia interagir não covalentemente com moléculas capazes de ligar ânions, como a hemoglobina. Essa condição nos levou a investigar as possíveis mudanças estruturais e funcionais das hemoglobinas bovina, humana e majoritária do peixe matrinxã (Brycon cephalus) quando interagem alostericamente com a glutationa. As amostras de sangue bovina e humana foram purificadas e submetidas à eletroforese para verificação de pureza. As propriedades de ligação com oxigênio e controle alostérico foram analisados por tonometria a 20°C, calculando a afinidade de ligação com o O2 e a cooperatividade (n50). As condições experimentais adotadas foram, stripped, cloreto e glutationa oxidada (GSSG), nessas condições, as hemoglobinas bovina e humana apresentaram efeito Bohr alcalino. O cloreto induziu o maior efeito de diminuição da afinidade em praticamente todas as condições. As hemoglobinas apresentaram processo cooperativo de ligação de oxigênio, em todas as condições e em toda faixa de pH. No caso da hemoglobina bovina adulta, a GSSG aumentou a afinidade por O2, em toda a faixa de pH testada, enquanto para a humana isso ocorreu abaixo de pH 7,0. O cloreto capaz de diminuir a afinidade de forma efetiva em todas as condições. A hemoglobina bovina apresentou uma menor afinidade de ligação ao oxigênio em relação à hemoglobina humana. A glutationa oxidada atuou como efetor alostérico heterotrópico em hemoglobinas humana, bovina e matrinxã (Hb-II), aumentando a afinidade de ligação por oxigênio da hemoglobina. Entretanto, a glutationa na forma reduzida... (Resumo completo, clicar acesso eletrônico abaixo)
Abstract: Glutathione (GSH) is an intracellular tripeptide, which in its reduced form acts as an antioxidant, keeping the cysteines in the reduced state. When exerting protective function, glutathione is oxidized to form its disulfide, exposing four negative charges. The oxidized glutathione (GSSG) could interact with molecules covalently able to bind anions, such as hemoglobin. That motivated us to investigate the possible structural and functional changes of bovine, human and a fish hemoglobin from the fish 'matrinxã' (Brycon cephalus) when they interact allosterically with glutathione. Samples of human and cattle blood were purified and subject to electrophoresis to verify their purity. The functional properties of oxygen binding and allosteric control were analyzed by the tonometric method at 20°C, calculating the affinity of O2-binding and cooperativity (n50). The tested experimental conditions involved hemoglobin in the absence (stripped) and in the presence of chloride and oxidized glutathione (GSSG). Under those circumstances, the human and bovine hemoglobins displayed an alkaline Bohr effect. Chloride induced the greatest effect of reducing affinity in all conditions. For all the experimental sets oxygen binding was cooperative. For bovine adult hemoglobin GSSG increased O2-affinity for all the tested pH values, whereas it occurred for human Hb for pH values above 7.0. Bovine Hb displayed lower O2-affinity than its human counterpart. Oxidized glutahione acted as a heterotropic allosteric effector in all the tested hemoglobins, increasing O2-affinity. However, GSH decreased O2-affinity of human and bovine Hbs. We assume that there is a binding site for GSSG at the R state, increasing O2-affinity, and another one for GSH at the T state, stabilizing its conformation and therefore lowering O2-affinity.
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Repetti, Leandro [UNESP]. „Possíveis associações entre marcadores genético-bioquímicos e sensibilidade a mastite em vacas da raça holandês, pura por cruzamento, variedade malhada de preto, em ambiente tropical“. Universidade Estadual Paulista (UNESP), 2003. http://hdl.handle.net/11449/95347.
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repetti_l_me_botfmvz.pdf: 176079 bytes, checksum: be20a2b4bea8e875acd51fdecc8bce0e (MD5)A mastite é um processo inflamatório da glândula mamária, aguda ou crônica, freqüente em ruminantes, sendo consideráveis as perdas econômicas por tal patologia, por desencadear inúmeros problemas sanitários para a pecuária leiteira. Portanto, a análise do polimorfismo dessas proteínas constitui-se numa importante ferramenta para o melhoramento genético do rebanho leiteiro. Neste trabalho, foram analisadas possíveis associações entre o polimorfismo bioquímico das hemoglobinas, transferrinas, albuminas séricas e beta lactoglobulinas e freqüência de mastite em vacas da raça Holandês, num rebanho controlado, mantidas em ambiente tropical. Embora não tenha sido constatada diferença significativa entre as freqüências de polimorfismo bioquímico das proteínas entre as duas populações estudadas, propõe-se a realização de novos estudos na área de biologia genética para que os dados que forem obtidos poderão ser empregados na orientação de programas de manejo e de melhoramento com vistas à resistência a mastite.
Mastitis is an inflammatory process of the mammary gland, sharp or chronic; frequent in ruminant, being considerable the economical losses for such pathology, for unchaining countless sanitary problems for the livestock milk pan. Therefore, the analysis of polymorphism of those proteins is constituted of an important tool for the flock milkman's genetic improvement. In this work, possible associations were analyzed among the biochemical polymorphism of the hemoglobins, transferrins, serum albumins and beta lactoglobulins and mastitis frequency in cows of the Dutch race, in a controlled flock, maintained in tropical atmosphere. Although it has not been verified significant differences among the frequencies of biochemical polymorphism of the proteins among the two studied populations, intends the accomplishment of new studies in the area of genetic biology so that the data that be obtained can be used in the orientation of handling programs and of improvement with views to the resistance the mastitis.
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Repetti, Leandro 1975. „Possíveis associações entre marcadores genético-bioquímicos e sensibilidade a mastite em vacas da raça holandês, pura por cruzamento, variedade malhada de preto, em ambiente tropical /“. Botucatu, [s.n.], 2003. http://hdl.handle.net/11449/95347.
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Orientador: Paulo Roberto Rodrigues RamosResumo: A mastite é um processo inflamatório da glândula mamária, aguda ou crônica, freqüente em ruminantes, sendo consideráveis as perdas econômicas por tal patologia, por desencadear inúmeros problemas sanitários para a pecuária leiteira. Portanto, a análise do polimorfismo dessas proteínas constitui-se numa importante ferramenta para o melhoramento genético do rebanho leiteiro. Neste trabalho, foram analisadas possíveis associações entre o polimorfismo bioquímico das hemoglobinas, transferrinas, albuminas séricas e beta lactoglobulinas e freqüência de mastite em vacas da raça Holandês, num rebanho controlado, mantidas em ambiente tropical. Embora não tenha sido constatada diferença significativa entre as freqüências de polimorfismo bioquímico das proteínas entre as duas populações estudadas, propõe-se a realização de novos estudos na área de biologia genética para que os dados que forem obtidos poderão ser empregados na orientação de programas de manejo e de melhoramento com vistas à resistência a mastite.
Abstract: Mastitis is an inflammatory process of the mammary gland, sharp or chronic; frequent in ruminant, being considerable the economical losses for such pathology, for unchaining countless sanitary problems for the livestock milk pan. Therefore, the analysis of polymorphism of those proteins is constituted of an important tool for the flock milkman's genetic improvement. In this work, possible associations were analyzed among the biochemical polymorphism of the hemoglobins, transferrins, serum albumins and beta lactoglobulins and mastitis frequency in cows of the Dutch race, in a controlled flock, maintained in tropical atmosphere. Although it has not been verified significant differences among the frequencies of biochemical polymorphism of the proteins among the two studied populations, intends the accomplishment of new studies in the area of genetic biology so that the data that be obtained can be used in the orientation of handling programs and of improvement with views to the resistance the mastitis.
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Nogueira, Nadir do Nascimento. „Utilização de biscoito fortificado com concentrado de hemoglobina bovina na dieta de pré-escolares. Efeito no estado de nutrição em ferro“. Universidade de São Paulo, 1991. http://www.teses.usp.br/teses/disponiveis/9/9132/tde-30082012-110522/.
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Biscoitos à base de farinha de trigo foram preparados com a adição de 3% de concentrado de hemoglobina bovina, obtido pela técnica de secagem de sangue animal em \"leito de jorro\", e introduzidos na dieta de pré-escolares de uma creche em Teresina, Estado do Piauí, Brasil. O estado de nutrição em ferro foi avaliado antes e após a intervenção A análise da dieta consumida mostrou déficit calórico e de ferro de 60 e 40%, respectivamente, bem como adequação quantitativa de proteína. A prevalência de anemia por deficiência de ferro foi de 75% (Hb < 11 g/dl), sendo 41% destes de grau severo (Hb < 9,3 g/dl). Com a introdução na dieta de 5 biscoitos/dia (5mg Fe), durante 90 dias, houve repleção hemoglobínica (Hb > 11 g/dl) em 100% das crianças.Wheat flour biscuits were prepared with the addition of 3% bovine hemoglobin concentrate obtained by the drying of animal blood in a spouted bed and were introduced in the diet of pre-school children from a kindergarten of Teresina, Piauí state, Brazil. Iron nutriture was evaluated before and after the intervention. The analysis of the diet consumed by the children showed energy and iron deficiencies of 40% and 60% respectively and a quantitative protein adequacy. The prevalence of iron deficiency anemia was 75% (Hb < 11 g/dl), 41% of these, of severe degree (Hb < 9,3 g/dl). With the introduction in the diet of 5 biscuits a day (5 mg Fe) for 90 days, there was hemoglobin repletion (Hb > 11 g/dl) in 100% of the children.
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Dimino, Michael Louis. „Synthesis, characterization, and modeling of novel bovine hemoglobin-based oxygen carriers“. 2007. http://etd.nd.edu/ETD-db/theses/available/etd-04032007-132849/.
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Thesis (Ph. D.)--University of Notre Dame, 2007.Thesis directed by Andre F. Palmer for the Department of Chemical and Biomolecular Engineering. "April 2007." Includes bibliographical references (leaves 111-123).
Buchteile zum Thema "Bovine hemoglobin"
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Fronticelli, Clara, und Enrico Bucci. „[10] Conformational and functional characteristics of bovine hemoglobin“. In Hemoglobins Part B: Biochemical and Analytical Methods, 150–63. Elsevier, 1994. http://dx.doi.org/10.1016/0076-6879(94)31012-2.
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Rentko, Virginia T., L. Bruce Pearce, Paula F. Moon-Massat und Maria S. Gawryl. „Hemopure® (HBOC-201, Hemoglobin Glutamer-250 (Bovine)): Preclinical Studies“. In Blood Substitutes, 424–36. Elsevier, 2006. http://dx.doi.org/10.1016/b978-012759760-7/50046-9.
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Pearce, L. Bruce, Maria S. Gawryl, Virginia T. Rentko, Paula F. Moon-Massat und Carl W. Rausch. „HBOC-201 (Hemoglobin Glutamer-250 (Bovine), Hemopure®): Clinical Studies“. In Blood Substitutes, 437–50. Elsevier, 2006. http://dx.doi.org/10.1016/b978-012759760-7/50047-0.
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Chen, Gang, und Thomas Ming Swi Chang. „Dual Antioxidant and Pro-Oxidation Effects of Ascorbic Acid on Bovine Hemoglobin“. In Nanobiotherapeutic Based Blood Substitutes, 571–95. WORLD SCIENTIFIC, 2022. http://dx.doi.org/10.1142/9789811228698_0023.
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Allchin, Douglas. „Nobel Ideals and Noble Errors“. In Sacred Bovines. Oxford University Press, 2017. http://dx.doi.org/10.1093/oso/9780190490362.003.0017.
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Christiaan Eijkman shared a 1929 Nobel Prize “for his discovery of the antineuritic vitamin.” His extensive studies on chickens and prison inmates on the island of Java in the 1890s helped establish a white rice diet as a cause of beriberi, and the rice coating as a remedy. Eijkman reported that he had traced a bacterial disease, its toxin, and its antitoxin. Beriberi, however, is a nutrient deficiency. Eijkman was wrong. Ironically, Eijkman even rejected the current explanation when it was first introduced in 1910. Although he earned a Nobel Prize for his important contribution on the role of diet, Eijkman’s original conclusion about the bacterium was just plain mistaken. Eijkman’s error may seem amusing, puzzling, or even downright disturbing—an exception to conventional expectations. Isn’t the scientific method, properly applied, supposed to protect science from error? And who can better exemplify science than Nobel Prize winners? If not, how can we trust science? And who else is to serve as role models for students and aspiring scientists? Eijkman’s case, however, is not unusual. Nobel Prize–winning scientists have frequently erred. Here I profile a handful of such cases (Figure 11.1). Among them is one striking pair, Peter Mitchell and Paul Boyer, who advocated alternative theories of energetics in the cell. Each used his perspective to understand and correct an error of the other! Ultimately, all these cases offer an occasion to reconsider another sacred bovine—that science is (or should be) free of error, and that the measure of a good scientist is how closely he or she meets that ideal. Consider first Linus Pauling, the master protein chemist. Applying his intimate knowledge of bond angles, he deciphered the alpha-helix structure of proteins in 1950, which earned him a Nobel Prize in 1954. He also reasoned fruitfully about sickle cell hemoglobin, leading to molecular understanding of its altered protein structure. Yet Pauling also believed that megadoses of vitamin C could cure the common cold. Evidence continues to indicate otherwise, although Pauling’s legacy still seems to shape popular beliefs.
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Allchin, Douglas. „Monsters and the Tyranny of Normality“. In Sacred Bovines. Oxford University Press, 2017. http://dx.doi.org/10.1093/oso/9780190490362.003.0025.
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In the sixteenth and seventeenth centuries, monsters were wonders (essay 1). Anomalous forms—like conjoined twins, hermaphrodites (essay 16), hydrocephalic babies, or the extraordinarily hairy Petrus Gonsalus and his equally hairy children—amazed people. They evoked a spirit of inquiry that helped fuel the emergence of modern science. Today, however, such bodies tend to strike us as freakish or grotesque—possibly even “against nature.” How did our cultural perspective, and with it, our values and emotional responses, change so radically? The shift in cultural views, ironically, paralleled deepening scientific understanding. Exceptions and anomalies can be powerful investigative tools. In this case, human monsters eventually prompted a new science, teratology, which compared normal and abnormal development. The scientific explanations and categories seemed to support value judgments. The history of monsters helps reveal the roots of a common belief (another sacred bovine): that the “normal” course of events reflects nature’s fundamental order. Well construed, monsters can help us rethink the meanings of normality and of the concept of laws of nature. Monsters are fascinating, of course, because they do not fit customary expectations. Such exceptions can be valuable opportunities for interpreting the unexceptional. One can begin to look for the relevant differences that reflect the underlying cause in both cases. It is a classic research strategy, especially in biology. Loss or modification of a structure can highlight its function. So, for example, vitamins were discovered through vitamin deficiency diseases, such as scurvy and beriberi. Likewise, the role of proteins in gene expression emerged from studying heritable enzyme deficiencies, such as alkaptonuria and phenylketonuria. Sickle cell anemia has become a classic example for learning in part because it was important historically in understanding hemoglobin and protein structure as well as the evolutionary consequences of the multiple effects of a single gene. Similarly, diabetes provides insight into the physiology of regulating blood glucose and the hormone insulin. Slips of the tongue are clues to how the brain processes language (missed notes in playing piano, too!).
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Jahr, Jonathan S., Kelly Tseng, Adam P. Brown und Gregory P. Dubé. „Hemoglobin-glutamer 250 (Bovine) [HBOC-201, Hemopure®] Clinical Use in South Africa and Comprehensive Review of Cardiac Outcomes and Risk/Benefit in Peer-Reviewed, Indexed Studies in Humans and Animal Models“. In Nanobiotherapeutic Based Blood Substitutes, 207–47. WORLD SCIENTIFIC, 2022. http://dx.doi.org/10.1142/9789811228698_0008.
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Guo, Chen, und Thomas Ming Swi Chang. „Long Term Safety and Immunological Effects of a Nanobiotherapeutic, Bovine Poly-[hemoglobin-catalase-superoxide dismutase-carbonic anhydrase], After Four Weekly 5% Blood Volume Toploading Followed by a Challenge of 30% Exchange Transfusion“. In Nanobiotherapeutic Based Blood Substitutes, 637–66. WORLD SCIENTIFIC, 2022. http://dx.doi.org/10.1142/9789811228698_0026.
Der volle Inhalt der QuelleKonferenzberichte zum Thema "Bovine hemoglobin"
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Franceschini, Maria Angela, Sergio Fantini, Albert Cerussi, Beniamino Barbieri, Britton Chance und Encico Gratton. „The Effect of Water in the Quantitation of Hemoglobin Concentration in a Tissue-Like Phantom by Near-Infrared Spectroscopy“. In Biomedical Optical Spectroscopy and Diagnostics. Washington, D.C.: Optica Publishing Group, 2006. http://dx.doi.org/10.1364/bosd.1996.ap16.
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We have investigated the contribution of water in the quantitative determination of hemoglobin concentration and saturation by near-infrared spectroscopy in turbid media. Our study consists of in vitro measurements on an aqueous suspension containing Liposyn, bovine blood, and yeast, buffered at pH 7.2. The optical coefficients of the medium (μ a ,~0.03-0.08 cm−1, μ s ′ ~0 cm−1) match those of biological tissue in the near-infrared, and the hemoglobin concentration (23 μM) is also similar to that found in tissues. We were able to reversibly saturate and desaturate hemoglobin in the full range O-100% by flowing either oxygen or nitrogen through the medium. We found that water absorption must be taken into account to obtain accurate results of hemoglobin concentration and saturation. However, for the two wavelengths employed in this study (715 and 825 nm), the water correction has a small effect on deoxy-hemoglobin concentration, and on hemoglobin saturation in the high saturation limit. Oxy-hemoglobin concentration, and hemoglobin saturation in the low saturation limit are the parameters most sensitive to water correction.
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Reinoso, Zain Sanchez, Jacinthe Thibodeau, Laila Ben Said, Ismail Fliss, Laurent Bazinet und Sergey Mikhaylin. „Bioactive Peptide Production from Slaughterhouse Blood Proteins: Impact of Pulsed Electric Fields and Ph on Enzyme Inactivation, Antimicrobial and Antioxidant Activities of Peptic Hydrolysates from Bovine and Porcine Hemoglobins“. In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/fsht2150.
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Slaughterhouse blood is a valuable by-product since multiple bioactive compounds can be derived out of it. Its solid fraction consists mainly of hemoglobin, which is a good source of antimicrobial and antioxidant peptides that can be released by peptic hydrolysis. Nevertheless, this method has limitations such as low yield, expensive cost of enzyme process, and non-eco-friendly production (high energy consumption and chemical reagents requested). Amount the alternative green technologies for protein valorization, pulsed electric field (PEF) stands out since it allows modifying the physicochemical properties of proteins, promoting the enzymatic hydrolysis, enzyme inactivation, and bioactivity enhancement. Thus, this study aimed to evaluate the effect of PEF on the pepsin inactivation and biological activities (antimicrobial and antioxidant) in hemoglobin hydrolysates. Bovine and porcine hemoglobins were hydrolyzed with pepsin for 3 h (37°C, pH 3.0) and treated with PEF (73 pulses, 23.8kV/cm, 90Hz) to inactivate the enzyme. The hydrolysis degree was evaluated, which did not show significant changes after PEF-inactivation of pepsin, whereas the peptide population analysis by RP-UPLC-MS/MS showed some changes in PEF-treated hydrolysates over time, which suggested a residual pepsin activity. Additionally, the impact of pH (3, 7, and 10) on bioactivity was studied. PEF-treatments did not show a significant impact on antimicrobial (antibacterial, antifungal, and anti-yeast activities) and antioxidant activities (DPPH and ORAC). However, higher pH fostered stronger anti-yeast activity (R. mucilaginosa) and DPPH‐scavenging capacity, whereas pH 7 fostered the antifungal activity (M. racemosus). Even though some changes were observed in the peptide population, no negative effects of PEF were found for biological activities. Thus, the utilization of hemoglobin from the meat industry combined with PEF-treatment fits the circular economy concept since derived peptides can be recycled to protect meat and other products against microbial growth and oxidation.
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Wu, Haizhou, Cecilia Tullberg und Ingrid Undeland. „Formation of reactive aldehydes (MDA, HHE, HNE) during in vitro digestion of cod muscle: role of hemoglobin from trout and bovine sources“. In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/jkrq2423.
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Heme-mediated oxidation in red meat is described as one of the potential routes to meat-induced colorectal cancer, which is linked to the ability of this reaction to continue also during gastrointestinal (GI) digestion while generating reactive aldehydes such as e.g. malondialdehyde (MDA), 4-hydroxy-2-nonenal (HNE) and 4-hydroxy-trans-2-hexenal (HHE). Very little is however known about the specific forms of heme being present at different stages of the GI-tract, and how mammal heme-proteins compare to those of for example fish with respect to their lipid pro-oxidative activity under GI-conditions. In the present study, the degradation of trout and bovine Hb and their pro-oxidant activities towards washed cod muscle mince were studied using in vitro GI digestion models. When the two Hb´s were subjected only to the pH-cycle of the GI-digestion model (pH 7→6→3→7) at 37°C, metHb formation increased following the initial gastric acidification to pH 6, especially for trout Hb. Subsequent acidification to pH 3 promoted Hb unfolding and partial or complete loss of the heme group. When digesting the Hb´s in the full digestion model, i.e. with enzymes and bile present, high-performance size-exclusion chromatography (HP-SEC) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of digests showed more extensive Hb-degradation in the gastric phase compared to in the duodenal phase. When washed cod muscle was digested without/with Hb, a strong pro-oxidative effect was seen from the Hb´s, resulting in high MDA, HHE, HNE formation which peaked at the end of the gastric phase. Slightly higher oxidation was seen with trout Hb, especially with respect to HHE. Results thus indicate that partially degraded Hb, and/or free hemin -both from mammal and fish sources- were highly pro-oxidative towards PUFA-rich lipids under GI-conditions, especially in the gastric phase.
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ABOU DIAB, Mira, Laurent Bazinet und Naima Nedjar. „Development of a New Innovative Process for the Production of Bioactive Peptides Resulting from the Enzymatic Hydrolysis of Bovine Hemoglobin: Electrodialysis with Bipolar Membranes“. In Virtual 2021 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2021. http://dx.doi.org/10.21748/am21.212.
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