Relevant bibliographies by topics / Fast protein liquid chromatography

Academic literature on the topic 'Fast protein liquid chromatography'

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Published: 4 June 2021
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Journal articles on the topic "Fast protein liquid chromatography"

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Cho, A.-Young, Giyoung Kim, Jongguk Lim, Changyeun Mo, Ji-Hea Moon, SaetByeol Park, Su-Hee Park, and Aeson Om. "Separation of Staphylococcal Enterotoxin B by Fast Protein Liquid Chromatography." Food Engineering Progress 19, no. 2 (May 31, 2015): 111–16. http://dx.doi.org/10.13050/foodengprog.2015.19.2.111.

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TAKAHASHI, Sadao, Toshitaka TAMAI, Hirotada TAKAI, Shinta HAYASHI, Hajime MAEDA, Hiroyuki SAGE, Tsuguhiko INAKA, and Susumu MIYABO. "Lipoproteins Separation on Superose 6 Gel-Filtration Column Using Fast Protein Liquid Chromatography System." Journal of Japan Atherosclerosis Society 15, no. 5 (1987): 1179–83. http://dx.doi.org/10.5551/jat1973.15.5_1179.

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Chaplin, L. C. "Hydrophobic interaction fast protein liquid chromatography of milk proteins." Journal of Chromatography A 363, no. 2 (January 1986): 329–35. http://dx.doi.org/10.1016/s0021-9673(01)83753-5.

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RAHMAN, K., U. VOSS, P. J. NICHOLLS, and ALAN D. B. MALCOLM. "Nucleic acid purification by fast protein liquid chromatography." Biochemical Society Transactions 16, no. 3 (June 1, 1988): 368. http://dx.doi.org/10.1042/bst0160368.

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Leoni, Patricia, Paul Heyworth, and Anthony W. Segal. "Separation of phosphoproteins by fast protein liquid chromatography." Journal of Chromatography B: Biomedical Sciences and Applications 527 (January 1990): 152–57. http://dx.doi.org/10.1016/s0378-4347(00)82093-9.

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Cattan, Alex R., and Julian Smith. "Computer control of fast protein liquid chromatography (FPLC)." Computers in Biology and Medicine 20, no. 2 (January 1990): 95–101. http://dx.doi.org/10.1016/0010-4825(90)90031-j.

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Grøstad, M., R. Rej, and N. E. Huseby. "Mitochondrial aspartate aminotransferase determined by "Fast Protein Liquid Chromatography"." Clinical Chemistry 36, no. 2 (February 1, 1990): 348–50. http://dx.doi.org/10.1093/clinchem/36.2.348.

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Abstract We describe an improved separation of the isoenzymes of aspartate aminotransferase (EC 2.6.1.1), based on ion-exchange chromatography. Involving the "Fast Protein Liquid Chromatography" system (Pharmacia) with a MonoQ column, this rapid, reproducible method for quantifying the mitochondrial enzyme shows good resolution and sensitivity, and results correlate well with those by an established immunochemical method.
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Andrews, A. T., M. D. Taylor, and A. J. Owen. "Rapid analysis of bovine milk proteins by fast protein liquid chromatography." Journal of Chromatography A 348 (January 1985): 177–85. http://dx.doi.org/10.1016/s0021-9673(01)92451-3.

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Sanogo, T., D. Paquet, F. Aubert, and G. Linden. "Purification of αS1-Casein by Fast Protein Liquid Chromatography." Journal of Dairy Science 72, no. 9 (September 1989): 2242–46. http://dx.doi.org/10.3168/jds.s0022-0302(89)79354-1.

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Ekstrand, Bo, and Lennart Björck. "Fast protein liquid chromatography of antibacterial components in milk." Journal of Chromatography A 358 (January 1986): 429–33. http://dx.doi.org/10.1016/s0021-9673(01)90357-7.

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Dissertations / Theses on the topic "Fast protein liquid chromatography"

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Jones, Karen Lorraine. "Analysis of ferredoxin and flavodoxin in Anabaena and Trichodesmium using fast protein liquid chromatography." PDXScholar, 1988. https://pdxscholar.library.pdx.edu/open_access_etds/3812.

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Iron is an essential nutrient for growth of photosynthetic microorganisms such as cyanobacteria and algae. Iron is required for proteins involved in the important processes of carbon and nitrogen assimilation. Low concentrations of iron in cultures or natural waters can lead to iron limitation which affects many aspects of algal metabolism. In natural waters, iron limitation can have effects on the patterns and rates of primary productivity. The cellular content of certain proteins can be affected by media iron concentrations. Methods have been used that assay components of the cell as an indirect measure of iron nutritional status. For example, spectroscopy can be performed to determine the cellular concentration of iron-containing proteins involved in photosynthesis. Organisms grown in media that imitate natural conditions, or organisms collected from their natural habitat are usually dilute. Methods that assay iron nutritional status such as spectroscopy and column chromatography require large sample sizes which are difficult to obtain from natural samples. In addition, methods that utilize techniques such as immunology or radioactive labelling are complex and time-consuming. These considerations led to the necessity of developing a technique that would be simple, rapid and effective on dilute samples. The method developed here utilized fast protein liquid chromatography (FPLC), which fulfilled these requirements. A complete analysis could be done within two to three hours with minimal sample treatment. The FPLC was simple to operate and was effective on a sample containing less than 100 μg of protein. Some photosynthetic organisms, when iron-depleted, can produce the flavin-containing protein flavodoxin (Flv). This protein substitutes for the iron-containing protein ferredoxin (Fd) in Fd-dependent reactions such as the light-induced reduction of NADP. The FPLC technique identified and quantified, in relative terms, Fd and Flv in the cell. Optical spectroscopy was used to verify FPLC retention time assignments. The results illustrated how the FPLC could be used to observe the changes in relative Fd and Flv content as a function of media iron concentration in cultures of the cyanobacterium Anabaena grown in the laboratory. It was found that Fd content decreased and Flv content increased with decreasing media iron concentration. In addition, samples of the cyanobacterium Trichodesmium collected from the ocean near Barbados were analyzed using FPLC to assay relative Fd and Flv content. By analogy with Anabaena, Fd and Flv retention times were identified. Using this technique conclusions could be drawn regarding the changing iron nutritional status of Trichodesmium in its natural habitat .
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Nguyen, Nhung Phuong. "Axial Ligand Mutant: H229A." Digital Archive @ GSU, 2008. http://digitalarchive.gsu.edu/honors_theses/1.

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Many pathogenic bacteria use their iron acquisition mechanisms to live inside hosts. Streptococcus pyogenes is a pathogenic bacterium that uses streptococcal iron acquisition ABC transporter to obtain heme. SiaA (HtsA, spy1795), a lipoprotein located on the cell surface, serves as a heme binding protein. To understand the iron-uptake mechanism, histidine 229, one of the two proposed axial ligands in SiaA, was mutated to alanine. SiaA H229A was expressed in E. coli, lysed by French Press, and purified by fast protein liquid chromatography (FPLC). SDS-PAGE indicated that pure protein was isolated. Nickel affinity FPLC gave purer H229A when 0.5 M imidazole was added to the binding buffer. Overall, histidine 229 is likely to be an axial ligand in wild type SiaA, as shown by the fact the mutant readily lost heme as evidenced by UV-vis spectra.
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Kirk, John Daniel. "Particle beam LC/MS with fast atom bombardment." Thesis, Georgia Institute of Technology, 1990. http://hdl.handle.net/1853/27127.

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Edwardson, P. A. D. "High Performance Liquid Chromatography of polynucleotides and proteins." Thesis, London School of Hygiene and Tropical Medicine (University of London), 1987. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.376534.

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Smid, Jerusa. "Poliformismos do gene da proteína príon celular em pacientes com doença de Alzheimer." Universidade de São Paulo, 2011. http://www.teses.usp.br/teses/disponiveis/5/5138/tde-24052011-142607/.

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INTRODUÇÃO: Os polimorfismos do gene da proteína priônica (PRNP) podem estar associados a doenças neurológicas não priônicas. Estudos em pacientes com doença de Alzheimer (DA) apontam para possível associação entre os polimorfismos do códon 129 do PRNP e DA. Essa associação não foi estudada na população brasileira. Neste estudo, descrevemos a associação entre os diferentes polimorfismos do PRNP e DA. MÉTODOS: Foi estudada amostra composta por 100 pacientes com DA, acompanhados no Ambulatório de Neurologia Cognitiva e do Comportamento e no Centro de Referência em Distúrbios Cognitivos do Hospital das Clínicas da Faculdade de Medicina da Universidade de São Paulo, pareados para grupo controle com 111 indivíduos, em relação à frequência dos diferentes polimorfismos do PRNP e o desempenho cognitivo. Os polimorfismos do PRNP foram estudados pelo método de cromotografia líquida de fase reversa desnaturante (DHPLC). Foi realizada extratificação da amostra pelo genótipo da apolipoproteína E (apoE). RESULTADOS: A frequência dos polimorfismos do códon 129 foi: 45,5% M/M, 42,4% M/V e 12,2% V/V nos pacientes com DA; e 39,6% M/M, 50,5% M/V e 9,9% V/V nos indivíduos controles (p=0,503). O códon 117 apresentou variante alélica silenciosa em 5% dos pacientes com DA e 3% dos controles (p=0,780). A deleção de um ocatapeptídeo repetido ocorreu em 5% dos pacientes com DA e 4% dos controles (p=0,738). Todos os pacientes com DA e os controles eram N171N. Uma paciente do grupo com DA apresentou a mutação V180I. A análise bivariada e regressão logística não mostraram associação entre os diferentes polimorfismos do códon 129 e o desempenho cognitivo nos pacientes com DA, assim como nos indivíduos cognitivamente normais. A extratificação segundo genótipo da apoE não revelou diferença em relação aos polimorfismos do códon 129 do PRNP entre os grupos DA e controles. CONCLUSÕES: Não houve diferença de frequência dos diferentes polimorfismos do códon 129 do PRNP entre os pacientes com DA e idosos cognitivamente normais, bem como em relação aos demais códons polimórficos do gene. Não houve diferença em relação ao desempenho cognitivo nos pacientes com DA e nos controles segundo o polimorfismo do códon 129 do PRNP. Um paciente apresentou mutação do códon 180 (V180I), e recebeu o diagnóstico de doença de Creutzfeldt-Jakob genética
INTRODUCTION: The polymorphism in the prion protein gene (PRNP) may influence non prion neurological diseases. Some reports associate Alzheimers disease (AD) and the polymorphic codon 129 of the PRNP. This association has not been studied in Brazilian population. In this study we aimed to describe the association between the polymorphisms of codon 129 of the PRNP and AD. METHODS: One hundred AD patients were evaluated in the Cognitive and Behavioral Neurology Unit and Cognitive Disorders Reference Center of the Hospital das Clínicas of the University of São Paulo School of Medicine, matched for 111 controls, regarding to the PRNP polymorphism and cognitive measures. The PRNP polymorphisms were analyzed using denaturing high-performance liquid chromatography (DHPLC). Analyzes stratifying by apoE genotype was performed. RESULTS: The distribution of the codon 129 polymorphisms were: 45.5% M/M, 42.4% M/V and 12.2% V/V in AD patients; 39.6% M/M, 50.5% M/V and 9.9% V/V in the control group (p=0.503). The 117 codon analysis revealed silent allelic variant in 5% of AD patients and 3% of controls (p=0.780). The octarepeat deletion occurred in 5% of AD and 4% of controls (p=0.738). All AD patients and controls were N171N. One AD patient had a point mutation at codon 180 (V180I). Logistic regression failed to confirm any association between AD cognitive performance and the codon 129 of PRNP, as well as in the control group. There was no association between the codon 129 genotypes and genotypes and AD according to the apoE stratification. CONCLUSIONS: There were no differences in the frequency of the codon 129 polymorphism between AD. control group, according to the codon 129 polymorphisms. A point mutation at the codon 180 (V180I) was diagnosed in one patient
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Bian, Juan. "Liquid Chromatography and Mass Spectrometry Based Analytical Method Development Towards Fast and Sensitive Analysis." The Ohio State University, 2019. http://rave.ohiolink.edu/etdc/view?acc_num=osu1557242729134942.

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Ansong, Godfred. "Analysis of plant polyphenols by high performance liquid chromatography/mass spectrometry and protein binding." Oxford, Ohio : Miami University, 2004. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=miami1083081905.

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Zhou, Feng. "Protein characterization by capillary isoelectric focusing electrophoresis, reversed phase liquid chromatography and mass spectrometry." Access to citation, abstract and download form provided by ProQuest Information and Learning Company; downloadable PDF file, 103 p, 2008. http://proquest.umi.com/pqdweb?did=1456289241&sid=4&Fmt=2&clientId=8331&RQT=309&VName=PQD.

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Muir, Matthew Stewart. "Proteomics of the ovine cataract." Diss., Lincoln University, 2008. http://hdl.handle.net/10182/792.

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The lens of the eye needs to be completely transparent in order to allow all light entering the eye to reach the retina. This transparency is maintained by the highly ordered structure of the lens proteins the crystallins. Any disruption to the lens proteins can cause an opacity to develop which is known as cataract. During cortical cataract formation there is increased truncation of the lens crystallins. It is believed that overactivation of calcium-dependent cysteine proteases, the calpains, is responsible for the increased proteolysis of the crystallins seen during cataractogenesis. Within the ovine lens there are three calpains, calpain 1, 2 and the lens specific calpain Lp82. The aim of this thesis was to determine the changes in the lens proteins during ageing and cataractogenesis, and to establish the role of the calpains in these processes. Calpain 1 and 2 were purified from ovine lung and Lp82 was purified from lamb lenses using chromatography. Activity and presence of the calpains was determined by using the BODIPY-FL casein assay, gel electrophoresis, Western blot and casein zymography. Changes in the lens proteins, specifically the crystallins, were visualised using two-dimensional electrophoresis (2DE). Lenses from fetal, 6 month old and 8 year old sheep were collected, as well as stage 0, 1, 3 and 6 cataractous ovine lenses. The proteins from the lenses were separated into the water soluble and urea soluble fractions and analysed by 2DE. Mass spectrometry was used to determine the masses and therefore modifications of the crystallins. Finally, the individual crystallins were separated using gel filtration chromatography and incubated with the purified calpains in the presence of calcium. The extent of the proteolysis was visualised using 2DE and truncation sites determined by mass spectrometry. Purification of the calpains resulted in samples that were specific for each calpain and could be used in further experiments. 2DE analysis showed that there were changes to the crystallins during maturation of the lens. The α-crystallins become increasingly phosphorylated as the lens ages and a small amount becomes truncated. The β-crystallins were also modified during ageing by truncation and deamidation. When crystallins from cataractous lenses were compared using 2DE there were changes to both the α- and β-crystallins. The α-crystallins were found to be extensively truncated at their C-terminal tail. Four of the seven β-crystallins, βB1, βB3, βB2 and βA3, showed increased truncation of their N-terminal extensions during cataract formation. All three calpains truncated αA and αB-crystallin at their C-terminal ends after incubation. Calpain 2 and Lp82 each produced unique αA-crystallin truncations. All three calpains truncated βB1 and βA3 and calpain 2 also truncated βB3. When the truncations from the calpain incubations were compared to those seen during cataract formation, many of the truncations were found to be similar. Both the unique truncations from calpain 2 and Lp82 were found in cataractous lenses, with the Lp82 more obvious in the 2DE. The β-crystallin truncations found after incubation with the calpains were similar to those found during cataractogenesis. In conclusion this study documents the changes to the ovine lens during maturation and cataractogenesis and indicates a role for the calpain family in the increased proteolysis observed in the ovine cataract.
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Atkinson, Ian E. "Mass Spectrometric Analysis of Environmental Contaminants, Protein Structure and Expression." Cleveland State University / OhioLINK, 2008. http://rave.ohiolink.edu/etdc/view?acc_num=csu1231174291.

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Books on the topic "Fast protein liquid chromatography"

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Fast liquid chromatography-mass spectrometry methods in food and environmental analysis. London: Imperial College Press, 2015.

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1946-, Kastner Michael, ed. Protein liquid chromatography. Amsterdam: Elsevier, 2000.

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Protein Liquid Chromatography. Elsevier, 2000. http://dx.doi.org/10.1016/s0301-4770(08)x6027-0.

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Kastner, M. Protein Liquid Chromatography (Journal of Chromatography Library). Elsevier Science, 1999.

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Kastner. Protein Liquid Chromatography (Journal of Chromatography Library). Elsevier Science, 1999.

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Núñez, Oscar, Héctor Gallart-Ayala, Claudia P. B. Martins, and Paolo Lucci. Fast Liquid Chromatography–Mass Spectrometry Methods in Food and Environmental Analysis. IMPERIAL COLLEGE PRESS, 2014. http://dx.doi.org/10.1142/p950.

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Fieldflow Fractionation In Biopolymer Analysis. Springer, 2011.

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Caldwell, Karin D., and S. Kim R. Williams. Field-Flow Fractionation in Biopolymer Analysis. Springer, 2014.

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Book chapters on the topic "Fast protein liquid chromatography"

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Madadlou, Ashkan, Siobhan O’Sullivan, and David Sheehan. "Fast Protein Liquid Chromatography." In Methods in Molecular Biology, 365–73. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-6412-3_19.

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Madadlou, Ashkan, Siobhan O’Sullivan, and David Sheehan. "Fast Protein Liquid Chromatography." In Methods in Molecular Biology, 439–47. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-913-0_25.

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Ardö, Ylva. "Separation of Peptidases Using Fast Protein Liquid Chromatography (FPLC)." In MILK the vital force, 191–93. Dordrecht: Springer Netherlands, 1986. http://dx.doi.org/10.1007/978-94-009-3733-8_161.

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Wilbert, D. M., M. Schauer, and G. H. Jacobi. "Determination of Nuclear Prostatic Androgen Receptors by FPLC (Fast Protein Liquid Chromatography)." In Investigative Urology 2, 99–106. Berlin, Heidelberg: Springer Berlin Heidelberg, 1987. http://dx.doi.org/10.1007/978-3-642-72735-1_16.

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Bai, Quan, and Xindu Geng. "Protein Folding Liquid Chromatography." In Methods in Molecular Biology, 69–85. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-61737-967-3_5.

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Stastna, Miroslava, and Jennifer Van Eyk. "Protein Separation: Liquid Chromatography." In Clinical Proteomics, 31–51. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2008. http://dx.doi.org/10.1002/9783527622153.ch3.

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Stroh, Justin G., and Kenneth L. Rinehart. "Liquid Chromatography/Fast Atom Bombardment Mass Spectrometry." In Experimental Mass Spectrometry, 287–306. Boston, MA: Springer US, 1994. http://dx.doi.org/10.1007/978-1-4899-2569-5_8.

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Kamp, Roza Maria. "High Performance Liquid Chromatography of Proteins." In Advanced Methods in Protein Microsequence Analysis, 21–33. Berlin, Heidelberg: Springer Berlin Heidelberg, 1986. http://dx.doi.org/10.1007/978-3-642-71534-1_3.

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Jervis, L. "Fast Analytical Dye-Ligand Chromatography in Process Development." In Protein-Dye Interactions: Developments and Applications, 121–23. Dordrecht: Springer Netherlands, 1989. http://dx.doi.org/10.1007/978-94-009-1107-9_13.

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Moritz, Robert L., and Richard J. Simpson. "Capillary Liquid Chromatography: A Tool for Protein Structural Analysis." In Methods in Protein Sequence Analysis, 3–10. Boston, MA: Springer US, 1993. http://dx.doi.org/10.1007/978-1-4899-1603-7_1.

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Conference papers on the topic "Fast protein liquid chromatography"

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Freeman, L., V. Hornsey, D. S. Pepper, P. R. Foster, L. Winkelman, and J. Dawes. "PROTEIN AGGREGATES IN HEATED BLOOD PRODUCTS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644019.

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Heating of blood products to reduce viral infectivity is now a standard practice. Such treatment may also modify the constituent proteins, reducing their activity or altering their structure with potentially harmful consequences for the recipient. Partially denatured proteins frequently form aggregates, which are often immunogenic and could precipitate immune complex formation, allergic reactions and kidney damage. In addition they may contribute to the development of AIDS after HIV infection by inducing a persistent state of T-cell activation.Protein aggregate formation in factor VIII and factor IX (II + X) concentrates has been investigated by fast protein liquid chromatography (FPLC), which proved to be a rapid, convenient method for this purpose. Freeze-drying alone resulted in aggregate formation in intermediate purity FVIII concentrates, but not in FIX concentrates. However, aggregates were detected after heating the FIX concentrate at 80°C for 72h in the dry state. Dry heating of intermediate purity FVIII concentrates to 68°C for 24h also increased the content of protein aggregates, which contained fibrinogen and fibronectin but little IgG. In this product, the aggregate content after heating correlated with total protein concentration. A higher purity FVIII concentrate selectively depleted in fibrinogen and fibronectin also contained protein aggregates after freeze-drying, but heating this product at 80°C for 72h resulted in a relatively small increase in aggregate content. Haemophiliacs receiving regular injections of heated concentrates are constantly exposed to protein aggregates. They should be monitored for any harmful effects, and manufacturers should aim to reduce the aggregate content of their products.
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Kimmel, Jeremy D., Christopher S. Lacko, Russell L. Delude, and William J. Federspiel. "Dynamics of TNF Capture Within Hemoadsorption Beads Used to Treat Sepsis." In ASME 2010 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2010. http://dx.doi.org/10.1115/sbc2010-19242.

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Sepsis is a serious medical condition characterized by systemic inflammation caused by infection, and affects more than 750,000 individuals per year in the US, with a mortality rate of approximately 30% [1]. The pathophysiology of sepsis is complex and not entirely understood, but is believed to be related to the dysfunction of multiple interdependent humoral mediator pathways, including redundant release of inflammatory cytokines [2]. Removal of both pro- and anti-inflammatory cytokines from the circulating blood is believed to be a promising therapy for severe sepsis [3]. We are developing an extracorporeal hemoadsorption device to remove cytokines from the blood using a novel, biocompatible, sorbent bead technology. In this work, we examined the adsorption dynamics of tumor necrosis factor (TNF) within hemoadsorption beads using packed bed capture experiments and fast protein liquid chromatography (FPLC).
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Czerchaujski, L., V. Hornsey, C. Prowse, and H. Bessos. "CROSS-REACTIV7E Fl/III :C IN THE RABBIT: A POTENTIAL ANIMAL MODEL FOR FUIII:C STUDIES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644036.

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A one step Enzyme-linked immunosorbent assay (ELISA) incorporating two anti-human FVIII :Ag monoclonal antibodies (MAbs) was used to determine FUIIIrAg in rabbits. Initial examinations showed the presence of cross-reactive FUIII:C in rabbit serum, plasma, and homogenates of normal rabbit liver, lung and spleen. Detailed investigation of normal rabbit plasma, and plasma depleted with Sephacryl S1000-anti FVIII :C MAbs and irrelevant MAbs (as control) using the ELISA, a chromogenic Fl/III:C activity assay, an immunoradiometric assay (IRMA) using human antibody, and fast protein liquid chromatography (FPLC) showed conclusively that the ELISA was specific for FVIII:C. The cross reactive FVIII:Ag was found to be most prominent in rabbit plasma, followed by serum, liver, lung and spleen. The ELISA should enable potential use of the rabbit as an animal model for FVIII:C studies, such as the enhancement of homologous FVIII:C with drugs or following tissue transplantation.
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Ingerslev, J., B. Sloth Christiansen, A. Bukh, S. Stenbjerg, T. Munck Jørgensen, and C. Munck Petersen. "HUMAN HEPATOCYTES CONTAIN HIGH MOLECULAR WEIGHT POLYPEPTIDES OF FACTOR VIII." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644324.

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Human hepatocytes were isolated by the two-step collagenase technique applied on distal left liver lobe. Homogenous and large cells were isolated revealing hepatocyte characteristics by light-microscopy. Hepatocytes were washed repeatedly in albumine buffer (5%), resuspended in the same buffer and sonicated using a cell density of 0.75 × 106 cells/ml. In some cases cells were separated from non-viable cells by flotation on a linear Percoll gradient. Supernate material after sonication was subjected to ELISA for VIII:Ag using human antibodies and vWf:Ag by polyclonal antibodies. Freshly isolated cells contained at least 0.25 IU/ 0.75 × 106 hepatocytes, whereas the vWf:Ag was below 0.01 IU/ 0.75 × 106 cells. The material obtained from sonication was further studied using fast protein liquid chromatography by Mono-Q HR 5/5 revealing a single peak of VIII: Ag eluting in the same position as the high molecular weight polypeptides of VIII :Ag of high purity FVIII derived from the plasma source. Isolated hepatocytes also were cultivated at 37°C in medium RPMI 1640 supplemented with Ultroser G (4%), glutamine and antibiotics. Cells secreted increasing quantities of albumin, fitrinogpn and protease-inhibitors. The supernatants also contained VIII: Ag in quantities ranging from 0.04 - 0.17 IU/ml after 24 hours, but no further secretion was observed. No vWf: Ag could be detected. Cells harvested and sonicated after 30 hours of culture only contained 0.04 IU/ 0.75 × 106 cells. Our results shows, that VIII :Ag is present in freshly isolated human hepatocytes and that only traces of vWf:Ag is found. A hepatocyte site of production of VIII is speculated. These very preliminary findings do not permit conclusions concerning active synthesis of VIII in hepatocytes. Further studies are underway.
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Henschen, A., and E. Müller. "ON THE FACTOR XIIIa-INDUCED CROSSLINKING OF HUMAN FIBRIN α-CHAINS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644649.

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Factor XIIIa catalysis the formation of isopeptide bonds Between γ-carbamoyl groups of peptide-bound glutamines and ε-amino groups of lysines or lysine analogues. During fibrin crosslinking two such bonds are rapidly formed between the C-termini of two γ-chains in adjacent molecules and then several bonds are more slowly formed between several α-chains. The crosslinking sites in the γ-chain were identified already 15 years ago, those in the α-chain are still only tentatively or partially identified,, However, by determining the incorporation of lysine analogues in the α-chain it could be shown that the glutamines in positions 328, 366 and possibly also 237 may participate in crosslinking reactions. Analyses of cyanogen bromide fragments isolated from crosslinked fibrin indicated the segments 271-776 and 518-587 to contain the primary crosslinking sites.In the present study factor XHI-containing fibrinogen was incubated over night with thrombin in presence of calcium ions and cysteine or, as a control, in presence of EDTA. The fibrin material was cleaved with cyanogen bromide, mercaptolysed, pyri-dylethylated and then subjected to Sephacryl S-300 chromatography. The early protein fractions were tested by reversed-phase high-performance liquid chromatography (HPLC) using fibrinogen fragments as reference. In the control sample Aa-chain fragment 271-776 eluted first but in the crosslinked sample it was missing and instead a heterogeneous mixture of higher-molecular weight components was observed. N-Terminal sequence analysis showed the mixture to contain not only the expected fragments 241-476 and 518-584,but in fact all glutamine- or lysine-containing Aα-chain fragments between positions 208 and 611. In the corresponding 6 fragments a total of 6 glutamines and 21 lysines as potential crosslinking sites are present. Two fragments contain only one each of these residues which therefore must be true crosslinking sites. Remaining sites and the actual linkages were identified after reversed-phase HPLC of the tryptic peptide mixture by N-terminal sequence and total amino acid analyses.The linkage pattern will provide information about the localisation and conformation of the C-terminal part of the α-chain and its contribution to the fibrin polymer structure.
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Tan, Yukun, Fernando B. Lima Neto, and Ulisses Braga Neto. "Inference of Protein-Protein Interaction Networks from Liquid-Chromatography Mass-Spectrometry Data by Approximate Bayesian Computation-Sequential Monte Carlo Sampling." In 2020 IEEE 30th International Workshop on Machine Learning for Signal Processing (MLSP). IEEE, 2020. http://dx.doi.org/10.1109/mlsp49062.2020.9231824.

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Dyr, J. E., H. Fořtová, J. Suttnar, Z. Vorlová, and F. Kornalxk. "ISOLATION OF HUMAN PROTEIN C AND ITS SNAKE VENOM ACTIVATORS BY ION EXCHANGE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644896.

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Simple and efficient methods for the purification of functionally active clotting factors in good yields are still missing. The purpose of the present study was to design a chromatographic procedure for the isolation of protein C (PC) and its snake venom activators taking advantage of the high resolution, high speed of analysis and sensitive detection of high performance liquid chromatography.PC was purified from a human plasma concentrate containing vitamin Kdependent proteins using a Mono Q anion exchanger. Electrophoretic titration curve was used to serve as a guide for finding approximate conditions for separations. Elution profiles for vitamin K-dependent proteins were determined. PC was assayed by both immunological and functional methods. For the latter methods, protein C activators (PCA) were isolated from snake venoms of Agkistrodon c, -contortrix (ACC) and Agkistrodon c, mokasen.Both venoms (pooled samples)were found to contain at least two different PCA. AtpH 6.5> by simple one step procedures either an acidic PCA (on a Mono Q) or a basic PCA (on a Mono S) was isolated. A great diversity was found among venom samples from specimen originating from a small geographic area near Philadelphia (USA). In six out of the nine analysed ACC venoms only the acidic PCA was present.In conclusion, an optimum separationof protein C onthe Mono Q at pH 8.0 was proposed (usual recovery 90-95%).Optimalization of the salt gradient was considerably more effective than the pH changes. A great individual variability has to be taken into account when snake venoms are used as a source of protein C activators.
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Sujatha, Lavanya Rai, Pratap Kumar, B. R. Krishnanand, K. K. Mahato, Sajan D. George, V. B. Kartha, and Santhosh C. "Protein profile study of Pap smear and tissue of cervix by high performance liquid chromatography: laser induced fluorescence." In Biomedical Optics (BiOS) 2007, edited by Daniel L. Farkas, Robert C. Leif, and Dan V. Nicolau. SPIE, 2007. http://dx.doi.org/10.1117/12.699711.

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Wang, Zhe, Biagio Mandracchia, Pietro Ferraro, Vincenzo Ferraro, Ernesto Di Maio, Pier Luca Maffettone, Wei-Chung Chen, and Eliot Fried. "Fast and Accurate Thickness Mapping of Liquid Bubbles and Thin Protein Films." In 2018 International Conference on Manipulation, Automation and Robotics at Small Scales (MARSS). IEEE, 2018. http://dx.doi.org/10.1109/marss.2018.8481180.

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Singh, Sameer Kumar, Remila L. Martis, Sujatha, Rani A. Bhat, Pralhad Kushtagi, Lavanya Rai, V. B. Kartha, and C. Santhosh. "Protein profile study of clinical samples of ovarian cancer using high-performance liquid chromatography-laser induced fluorescence (HPLC-LIF)." In Biomedical Optics 2006, edited by Jörg Enderlein and Zygmunt K. Gryczynski. SPIE, 2006. http://dx.doi.org/10.1117/12.647321.

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Reports on the topic "Fast protein liquid chromatography"

1

Jones, Karen. Analysis of ferredoxin and flavodoxin in Anabaena and Trichodesmium using fast protein liquid chromatography. Portland State University Library, January 2000. http://dx.doi.org/10.15760/etd.5696.

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