Gotowe bibliografie tematyczne / Fast protein liquid chromatography

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Gotowa bibliografia na temat „Fast protein liquid chromatography”

Autor: Grafiati
Data publikacji: 4 czerwca 2021
Data aktualizacji: 1 lutego 2022

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Artykuły w czasopismach na temat "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 та G. Linden. "Purification of αS1-Casein by Fast Protein Liquid Chromatography". Journal of Dairy Science 72, № 9 (вересень 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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Rozprawy doktorskie na temat "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 indi
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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 isolat
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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 Hospit
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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
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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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Książki na temat "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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Części książek na temat "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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Streszczenia konferencji na temat "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 fac
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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 a
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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 chromatogr
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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 isolate
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Henschen, A., та E. Müller. "ON THE FACTOR XIIIa-INDUCED CROSSLINKING OF HUMAN FIBRIN α-CHAINS". У 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
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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
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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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Raporty organizacyjne na temat "Fast protein liquid chromatography"

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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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