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Relevant bibliographies by topics / Protein A chromatography

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Academic literature on the topic 'Protein A chromatography'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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Journal articles on the topic "Protein A chromatography"

1

Mikšı́k, Ivan. "Protein liquid chromatography." Journal of Chromatography B: Biomedical Sciences and Applications 749, no. 1 (November 2000): 143–44. http://dx.doi.org/10.1016/s0378-4347(00)00366-2.

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Janson, Jan-Christer. "Practical protein chromatography." Journal of Biochemical and Biophysical Methods 26, no. 2-3 (May 1993): 244–45. http://dx.doi.org/10.1016/0165-022x(93)90050-x.

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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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Brocklehurst, Keith, Albert J. Courey, Sheraz Gul, Sue-Hwa Lin, and Robert L. Moritz. "Protein Ligand Affinity Chromatography." Cold Spring Harbor Protocols 2006, no. 1 (January 1, 2006): pdb.prot4203. http://dx.doi.org/10.1101/pdb.prot4203.

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Geng, Xindu, and Lili Wang. "Liquid chromatography of recombinant proteins and protein drugs." Journal of Chromatography B 866, no. 1-2 (April 2008): 133–53. http://dx.doi.org/10.1016/j.jchromb.2008.01.041.

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Shukla, Abhinav A., Priyanka Gupta, and Xuejun Han. "Protein aggregation kinetics during Protein A chromatography." Journal of Chromatography A 1171, no. 1-2 (November 2007): 22–28. http://dx.doi.org/10.1016/j.chroma.2007.09.040.

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KRUGER, J. E., and B. A. MARCHYLO. "SELECTION OF COLUMN AND OPERATING CONDITIONS FOR REVERSED-PHASE HIGH-PERFORMANCE LIQUID CHROMATOGRAPHY OF PROTEINS IN CANADIAN WHEAT." Canadian Journal of Plant Science 65, no. 2 (April 1, 1985): 285–98. http://dx.doi.org/10.4141/cjps85-041.

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Chromatographic conditions were optimized and three commercially available columns were evaluated for separation of alcohol-soluble storage proteins of Neepawa wheat using reversed-phase high-performance liquid chromatography (RP-HPLC). Optimal separation was achieved using an extracting solution of 50% 1-propanol, 1% acetic acid, and 4% dithiothreitol and an HPLC elution time of 105 min at a flow rate of 1.0 mL/min. HPLC columns evaluated (SynChropak RP-P, Ultrapore RPSC and Aquapore RP-300) varied in selectivity and resolution. The column providing the greatest versatility was Aquapore RP-300 available in cartridge form. Sodium dodecyl sulfate gradient-gel electrophoresis analysis of protein peaks resolved by RP-HPLC indicated that many of the eluted peaks contained more than one protein species. Chromatographic protein patterns obtained for Neepawa wheat grown at different locations and in different years were qualitatively the same.Key words: Protein, high-performance liquid chromatography, wheat

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Holm, Jan, Steen Ingemann Hansen, and Mimi Høier-Madsen. "A Combination of Cation Exchange and Ligand-Affinity Chromatography for Purification of Two Molecular Species of the Folate Binding Protein in Human Milk, One Equipped with a Hydrophobic Glycosyl Phosphatidylinositol Tail: Characterization of Hydrophobicity and Electrical Charge." Bioscience Reports 22, no. 3-4 (August 1, 2002): 443–54. http://dx.doi.org/10.1023/a:1020922226362.

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Cation exchange chromatography combined with ligand (methotrexate) affinity chromatography on a column desorbed with a pH-gradient was used for separation and large scale purification of two folate binding proteins in human milk. One of the proteins, which had a molecular size of 27 kDa on gel filtration and eluted from the affinity column at pH 5–6 was a cleavage product of a 100 kDa protein eluted at pH 3–4 as evidenced by identical N-terminal amino acid sequences and a reduction in the molecular size of the latter protein to 27 kDa after cleavage of its hydrophobic glycosylphosphatidyl-inositol tail that inserts into Triton X-100 micelles. Chromatofocusing showed that both proteins possessed multiple isoelectric points within the pH range 7–9. The 100 kDa protein exhibited a high affinity to hydrophobic interaction chromatographic gels, whereas this was only the case with unliganded forms of the 27 kDa protein indicative of a decrease in the hydrophobicity of the protein after ligand binding.

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Cassidy, Scott A., Linda J. Janis, and Fred E. Regnier. "Kinetic chromatographic sequential addition immunoassays using protein A affinity chromatography." Analytical Chemistry 64, no. 17 (September 1992): 1973–77. http://dx.doi.org/10.1021/ac00041a036.

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Gottstein, C., and R. Forde. "Affinity chromatography system for parallel purification of recombinant protein samples." Protein Engineering, Design and Selection 15, no. 10 (October 2002): 775–77. http://dx.doi.org/10.1093/protein/15.10.775.

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Dissertations / Theses on the topic "Protein A chromatography"

1

Cao, Liming. "Protein Separation with Ion-exchange Membrane Chromatography." Link to electronic thesis, 2005. http://www.wpi.edu/Pubs/ETD/Available/etd-050405-174109/.

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Hsu, Kuang-Hsin. "Scale-up of affinity chromatography for protein purifications." Ohio : Ohio University, 2000. http://www.ohiolink.edu/etd/view.cgi?ohiou1172002240.

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Ramat, Fabien M. "Protein purification using expanded bed chromatography." Digital WPI, 2004. https://digitalcommons.wpi.edu/etd-theses/92.

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Expanded bed chromatography using ion-exchange media is a powerful first step in purification processes. Expanded bed chromatography can be used to extract components from complex and viscous solution. This can be achieved because of the void created between adsorbent particles where as in packed bed chromatography, the adsorbent is too compact and dense for a complex feed stock to flow through. Expanded bed chromatography was used to purify bovine serum albumin (BSA) from chicken egg white (CEW). The high viscosity of CEW presents a unique challenge for efficient large-scale protein purification. This project aimed to optimize and evaluate a separation method that is believed to be particularly suitable for high viscosity solutions: expanded-bed ion exchange chromatography. The BSA was admixed into the CEW and the solution was pumped through the column for purification. The media used in the column was Streamline DEAE which is an anion-exchanger. The yield obtained was 85% and the purity was 57%. A mathematical model to understand and predict the behavior of expanded bed chromatography was developed to provide an estimation of the breakthrough curves obtained for BSA. A small sized porous dense adsorbent was also synthesized to enhance the purification process. This zirconia-based adsorbent allows use of higher flow velocities that is a key factor when working with viscous fluids such as chicken egg white.

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Batas, Borislav. "Protein refolding using size exclusion chromatography." Thesis, University of Bath, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.337817.

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Ramat, Fabien M. "Protein purification using expanded bed chromatography." Link to electronic thesis, 2003. http://www.wpi.edu/Pubs/ETD/Available/etd-0114104-114704.

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Thesis (M.S.)--Worcester Polytechnic Institute.
Keywords: zirconia; protein purification; anion exchange; chicken egg white; expanded bed chromatography. Includes bibliographical references (p. 83-86).

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Tuan, Chik Syed Mohd Saufi. "Mixed Matrix Membrane Chromatography for Bovine Whey Protein Fractionation." Thesis, University of Canterbury. Chemical and Process Engineering, 2010. http://hdl.handle.net/10092/3647.

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Whey protein fractionation is an important industrial process that requires effective large-scale processes. Although packed bed chromatography has been used extensively, it suffers from low processing rates due to high back-pressures generated at high flow rates. Batch chromatography has been applied but generally has a low efficiency. More recently, adsorptive membranes have shown great promise for large-scale protein purification, particularly from large-volume dilute feedstocks. A new method for producing versatile adsorptive membranes by combining membrane and chromatographic resin matrices has been developed but not previously applied to whey protein fractionation. In this work, a series of mixed matrix membranes (MMMs) were developed for membrane chromatography using ethylene vinyl alcohol (EVAL) based membranes and various types of adsorbent resin. The feasibility of MMM was tested in bovine whey protein fractionation processes. Flat sheet anion exchange MMMs were cast using EVAL and crushed Lewatit® MP500 (Lanxess, Leverkusen, Germany) anion resin, expected to bind the acidic whey proteins β-lactoglobulin (β-Lac), α-lactalbumin (α-Lac) and bovine serum albumin (BSA). The MMM showed a static binding capacity of 120 mg β-Lac g⁻¹ membrane (36 mg β-Lac mL⁻¹ membrane) and 90 mg α-Lac g⁻¹ membrane (27 mg α-Lac mL⁻¹ membrane). It had a selective binding towards β-Lac in whey with a binding preference order of β-Lac > BSA > α-Lac. In batch whey fractionation, average binding capacities of 75.6 mg β-Lac g⁻¹ membrane, 3.5 mg α-Lac g⁻¹ membrane and 0.5 mg BSA g⁻¹ membrane were achieved with a β-Lac elution recovery of around 80%. Crushed SP Sepharose™ Fast Flow (GE Healthcare Technologies, Uppsala, Sweden) resin was used as an adsorbent particle in preparing cation exchange MMMs for lactoferrin (LF) recovery from whey. The static binding capacity of the cationic MMM was 384 mg LF g⁻¹membrane or 155 mg LF mL⁻¹ membrane, exceeding the capacity of several commercial adsorptive membranes. Adsorption of lysozyme onto the embedded ion exchange resin was visualized by confocal laser scanning microscopy. In LF isolation from whey, cross-flow operation was used to minimize membrane fouling and to enhance the protein binding capacity. LF recovery as high as of 91% with a high purity (as judged by the presence of a single band in gel electrophoresis) was achieved from 150 mL feed whey. The MMM preparation concept was extended, for the first time, to produce a hydrophobic interaction membrane using crushed Phenyl Sepharose™ (GE Healthcare Technologies, Uppsala, Sweden) resin and tested for the feasibility in whey protein fractionation. Phenyl Sepharose MMM showed binding capacities of 20.54 mg mL⁻¹ of β-Lac, 45.58 mg mL⁻¹ of α-Lac, 38.65 mg mL⁻¹ of BSA and 42.05 mg mL⁻¹ of LF for a pure protein solution (binding capacity values given on a membrane volume basis). In flow through whey fractionation, the adsorption performance of the Phenyl Sepharose MMM was similar to the HiTrap™ Phenyl hydrophobic interaction chromatography column. However, in terms of processing speed and low pressure drop across the column, the benefits of using MMM over a packed bed column were clear. A novel mixed mode interaction membrane was synthesized in a single membrane by incorporating a certain ratio of SP Sepharose cation resin and Lewatit MP500 anion resin into an EVAL base polymer solution. The mixed mode cation and anion membrane chromatography developed was able to bind basic and acidic proteins simultaneously from a solution. Furthermore, the ratio of the different types of adsorptive resin incorporated into the membrane matrix could be customised for protein recovery from a specific feedstream. The customized mixed mode MMM consisting of 42.5 wt% of MP500 anionic resin and 7.5 wt% SP Sepharose cationic resin showed a binding capacity of 7.16 mg α-Lac g⁻¹ membrane, 11.40 mg LF g⁻¹ membrane, 59.21 mg β-Lac g⁻¹ membrane and 6.79 mg IgG g⁻¹ membrane from batch fractionation of 1 mL LF-spiked whey. A tangential flow process using this membrane was predicted to be able to produce 125 g total whey protein per L membrane per h.

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Polykarpou, E. "Optimisation of chromatography for downstream protein processing." Thesis, University College London (University of London), 2011. http://discovery.ucl.ac.uk/1334599/.

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Downstream bioprocessing and especially chromatographic steps, commonly used for the purification of multicomponent systems, are significant cost drivers in the production of therapeutic proteins. Lately, there has been an increased interest in the development of systematic methods where operating conditions are defined and chromatographic trains are selected. Several models have been developed previously, where chromatographic trains were selected under the assumption of 100% recovery of the desired product. Removing this assumption gives the opportunity not only to select chromatographic trains but also determine the timeline in which the product is selected. Initially, a mixed integer non-linear (MINLP) programming mathematical model was developed to tackle that problem and was tested using three illustrative examples. Later on, this model was linearised by applying piecewise linear approximation techniques and computational efficiency was improved. Next, an alternative MILP model was developed by discretising the recovery levels of the product and computational efficiency improved even by 100-fold. Finally, the equilibrium dispersive model was used in a simple 4-protein mixture and the MINLP model was validated. This research represents a significant step towards efficient downstream process operation and synthesis

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Conti, Sofia Alessandra. "Monoclonal antibodies purification via Protein G and protein A affinity chromatography." Master's thesis, Alma Mater Studiorum - Università di Bologna, 2021.

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realization of a pilot scale affinity protein G chromatography for the purification of small volumes of supernatant from different harvests from the same antibody clone. The objective was to make a study on the productivity of each harvest, investigating for a dilution effect in case of an increasing number of harvests, and to have a rapid retention kit for the quality control of the purified antibody. Moreover, an identical column packed with protein A has been tested with the same products, in order to see if there was space for a yield improvement, and a further scale-up.

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To, Chi Shung Brian. "Protein retention and transport in hydrophobic interaction chromatography." Access to citation, abstract and download form provided by ProQuest Information and Learning Company; downloadable PDF file 2.12 Mb., 319 p, 2006. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&res_dat=xri:pqdiss&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&rft_dat=xri:pqdiss:3205434.

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Johnson, David H. "High-throughput self-interaction chromatography applications in formulation prediction for proteins /." Birmingham, Ala. : University of Alabama at Birmingham, 2008. https://www.mhsl.uab.edu/dt/2009r/johnson.pdf.

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Thesis (M.S.)--University of Alabama at Birmingham, 2008.
Title from PDF title page (viewed Sept. 21, 2009). Additional advisors: Martha W. Bidez, W. Michael Carson, Richard A. Gray, W. William Wilson. Includes bibliographical references.

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Books on the topic "Protein A chromatography"

1

Walls, Dermot, and Sinéad T. Loughran, eds. Protein Chromatography. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-6412-3.

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Walls, Dermot, and Sinéad T. Loughran, eds. Protein Chromatography. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-60761-913-0.

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Kenney, Andrew, and Susan Fowell. Practical Protein Chromatography. New Jersey: Humana Press, 1992. http://dx.doi.org/10.1385/0896032132.

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Protein chromatography: Methods and protocols. New York, N.Y: Humana Press, 2011.

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Carta, Giorgio. Protein chromatography: Process development and scale-up. Weinheim: Wiley-VCH, 2010.

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Protein affinity tags: Methods and protocols. New York: Humana Press, 2014.

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Lan, Chi-Wei. Protein purification using fluidised bed chromatography: Physical and biochemical characterisation of a simple absorbent contactor. Birmingham: University of Birmingham, 2000.

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1945-, Nakanishi Kazuhiro, and Matsuno Ryūichi 1939-, eds. Ion-exchange chromatography of proteins. New York: M. Dekker, 1988.

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9

Staby, Arne, Anurag S. Rathore, and Satinder Ahuja, eds. Preparative Chromatography for Separation of Proteins. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2017. http://dx.doi.org/10.1002/9781119031116.

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P, Georgiev G., ed. Khromatografii͡a︡ belkov i nukleinovykh kislot. Moskva: Izd-vo "Nauka", 1985.

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Book chapters on the topic "Protein A chromatography"

1

Rosenberg, Ian M. "Chromatography." In Protein Analysis and Purification, 324–84. Boston, MA: Birkhäuser Boston, 1996. http://dx.doi.org/10.1007/978-1-4612-2056-5_10.

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Rosenberg, Ian M. "Chromatography." In Protein Analysis and Purification, 265–324. Boston, MA: Birkhäuser Boston, 1996. http://dx.doi.org/10.1007/978-1-4757-1108-0_10.

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Dennison, Clive. "Chromatography." In A Guide to Protein Isolation, 89–138. Dordrecht: Springer Netherlands, 2003. http://dx.doi.org/10.1007/978-94-017-0269-0_5.

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Urh, Marjeta, Danette Hartzell, Jacqui Mendez, Dieter H. Klaubert, and Keith Wood. "Methods for Detection of Protein–Proteinnl and Protein–DNA Interactions Using HaloTag ™." In Affinity Chromatography, 191–210. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-582-4_13.

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Boyer, Philip M., and James T. Hsu. "Protein purification by dye-ligand chromatography." In Chromatography, 1–44. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/bfb0046571.

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Jennissen, Herbert P. "Hydrophobic Interaction Chromatography." In Protein-Ligand Interactions, 81–99. Totowa, NJ: Humana Press, 2005. http://dx.doi.org/10.1007/978-1-59259-912-7_5.

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Wombacher, H., and L. Jacob. "Affinity Chromatography of Proteins." In Protein Structure Analysis, 11–30. Berlin, Heidelberg: Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-642-59219-5_2.

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Lee, Tzong-Hsien, and Marie-Isabel Aguilar. "Protein Separation Using Immobilized Phospholipid Chromatography." In Affinity Chromatography, 295–302. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-582-4_20.

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Zettlitz, Kirstin A. "Protein A/G Chromatography." In Antibody Engineering, 531–35. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-01144-3_34.

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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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Conference papers on the topic "Protein A chromatography"

1

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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Saufi, Syed M., and Conan J. Fee. "Batch adsorption of whey protein onto anion exchange mixed matrix membrane chromatography." In 2010 2nd International Conference on Chemical, Biological and Environmental Engineering (ICBEE). IEEE, 2010. http://dx.doi.org/10.1109/icbee.2010.5650595.

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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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TSUNEIZUMI, I., T. MEGURO, and K. YAMADA. "SUDAY ON A SUBSTANCE FUNCTIONALLY LIKE PROTEIN C IN PLASMA." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644303.

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The present report first deals with the isolation and characterization of a substance found to demonstrate protein C like activity(PCLA). When it was activated by thrombin, the PCLA substance prolonged the activated partial thromboplastin time(aPTT). The activated PCLA substance also hydrolyzed synthetic substrates such as S�2238, S�2366 and S�2266,while the PCLA substance was not cross reacted with anti-protein C serum(Behring Manheim). The PCLA substance was adsorbed by both aluminium hydroxide gel and barium sulfate. The level of Km, optimum pH and optimum I.S. in the amido-lytic reaction with synthetic substrate is shown in the table.In the chromatography of Sepharose CL-6B gel, the PCLA substance was eluted in the fraction of higher molecular weight, while protein C was eluted with a lower fraction.This prompts an estimate that the molecular weight of the PCLA substance is approximately 200,000. Through DEAE-Sepharose CL-6B gel ion exchange chromatography, the PCLA substance was eluted by a lower ionic strength than was protein C.The levels of a PCLA substance were low in the patients with a vitamin K deficiency and in newborn infants. It is expected that our findings regarding the PCLA substance will be as clinically significant as that which we know about protein C at present.

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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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Yang, Shiau-Jyun, and Yu-Kaung Chang. "Method Development for Extraction of GST-EGFP Fusion Protein by Immobilized Metal Affinity Chromatography." In 14th Asia Pacific Confederation of Chemical Engineering Congress. Singapore: Research Publishing Services, 2012. http://dx.doi.org/10.3850/978-981-07-1445-1_714.

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Fujikawa, K., T. Funakoshi, J. F. Tait, and R. L. Heimark. "PLACENTAL ANTICOAGULANT PROTEIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643912.

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An anticoagulant protein was purified from the soluble fraction of human placenta by ammonium sulfate precipitation and column chromatography on DEAE-Sepharose, Sephadex G-75, and mono S (Pharmacia). Approximately 30 mg of the protein was purified from one placenta. The purified protein gave a single band on SDS polyacrylamide gel and had a molecular weight of 36,500. This protein inhibited both kaolin and thromboplastin induced clotting times of normal human plasma. It also inhibited the clotting time of platelet-rich plasma induced by factor Xa, but did not affect thrombin activity of fibrinogen-fibrin conversion. The protein neither bound factor Xa nor inhibited the amidase activity of factor Xa. This protein specifically bound to phospholipid vesicles prepared from a mixture of phosphatidylserine and phosphatidylcholine (20 to 80 weight ratio) in the presence of calcium ions. The purified protein was digested with cyanogen bromide and the resulting fragments were separated by FPLC. Partial amino acid sequences of the cyanogen bromide fragments showed that this protein was composed of at least three repeats that were homologous to the four repeats found in lipocortin I and II. Lipocortins are known to inhibit the phospholipase A2 activity, probably by binding to the phospholipid substrate. These results indicate that the placental anticoagulant protein is a member of the family of lipocortins and probably inhibits coagulation by binding to phospholipid vesicles. Supported in part by grants HL 16919 and HL 18645 from National Institute of Health.

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Bhattacharya, Prabir, Carolyn L. Orthner, and Dudley K. Strickland. "DEVELOPMENT OF A PROTEIN C CONCENTRATE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644313.

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A Protein C (PC) concentrate may be useful in treating patients with congenital or acquired Protein C deficiencies. A method for preparation of a human Protein C concentrate has been developed using a by-product of American Red Cross Factor IX production as the starting material (Menache et. al. Blood, 64, 1220). Levels of other vitamin K dependent proteins in the Protein C concentrate were measured and found to be <10 units per 100 units of PC, except for Protein S. The level of Protein S as judged by immunological assay was 30 u/100 u PC. Assay of the PC concentrate using chrcmogenic substrates revealed that levels of thrombin, Factor 3�a and Factor IXa were less than 0.006 u/mL. In addition, Antithrombin III and ax -macroglobulin were not detected. The vivo effects of Protein C concentrate and Protein C activated by thrombin have been tested in anesthetized rabbits. Thrombin was removed from the activated Protein C by ion-exchange chromatography; depletion was verified by S-2238 or by a clotting assay (< 0.006 u/mL). Rabbits were injected with Protein C concentrate (400 ug/kg) or activated Protein C 24 - 48 ug/Kg). The activated partial thromboplastin time (APTT), FactorV (FV) and Factor VIII (FVIII) levels were measured in samples collected over the next three hours. Infusion of PC concentrate elevated the level of PC to 150% of the preinfusion level within 30 min. It did not change the levels of FV, FVIII, fibrinogen or platelet count. In contrast, infusion of activated Protein C produced progressive prolongation of the APTT. Levels of FV and FVIII were decreased to 25% and 50% of preinfusion levels, respectivelv, three hours after the infusion. Fibrinogen and platelet levels were unchanged during that period. These data demonstrate that activated human Protein C concentrate induces an anticoagulant effect that can be readily measured in rabbits.

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9

Newman, J., and D. Farb. "LARGE SCALE PREPARATION OF VON WILLEBRAND FACTOR BY AFFINITY CHROMATOGRAPHY." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644093.

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Treatment of bleeding in von Willebrand's disease usually consists of the infusion of cryoprecipitate or plasma. DDAVP is effective in some patients. Commercial concentrates for the treatment of Hemophilia A are ineffective as a source of von Willebrand Factor (vWF) replacement in von Willibrand's disease presumedly because of the absence of higher molecular weight forms of vWF protein. A vWF concentrate obtained during the course of preparation of an affinity purified Factor VIII may provide an alternative therapeutic agent without impacting the available Factor VIII supplies. The process used for the preparation of a highly purified Factor VIII concentrate (MonoclateTM, Armour Pharmaceutical Co.) from cryoprecipitate includes an affinity chromatography step which separates vWF/Factor VIII complex from other proteins in cryoprecipitate using an anti-vWF monoclonal antibody (C. A. Fulcher & T. S. Zimmerman, 1982). Factor VIII is then dissociated from the vWF remaining on the column and is eluted immediately by 3M sodium thiocyanante (NaSCN) as a step in the regeneration of the column. Unless the NaSCN is rapidly removed from the elutriant, the vWF activity as measured by platelet agglutination is destroyed. We have taken the NaSCN eluate and processed it immediately over an in-line G-10 or G-25 Sephadex column which removes the NaSCN while the vWF is eluted with a buffered isotonic solution. Alternatively, the vWF has been precipitated from the NaSCN by ammonium sulfate or polyethylene glycol. VWF prepared by any of these methods retains platelet agglutinating activity and has a distribution of vWF multimers similar to those of vWF in normal plasma.The potency of vWF prepared from cryoprecipitate by this process is 20 units/ml and the specific activity is 20 units/mg. In several fractionations of kilogram amounts of cryoprecipitate, vWF was isolated and subjected to lyophilization and heating at 68° for 30 hours without loss of bioactivity. Drug development in progress suggest that the combined effect of affinity chromatography and exposure to NaSCN may negate the need for a heating procedure to reduce the risk of viral transmittance.

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10

Varela, D., R. O’Hara, and A. C. Neves. "BY-PRODUCTS OF THE WHELK PROCESSING INDUSTRY AS VALUABLE SOURCE OF ANTIOXIDANT PEPTIDES." In World Conference on Waste Management. The International Institute of Knowledge Management, 2021. http://dx.doi.org/10.17501/26510251.2021.1103.

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The fish and shellfish industry processes 851,984 tonnes of fish per year worldwide. However, only 43% of that is consumed, and valuable proteins are processed as waste. Protein hydrolysates are widely used in food technology for their nutritional and functional properties. The goal of this project is to extract protein from whelk by-products derived from the shellfish processing industry and create protein hydrolysates that have marketable value. The by-products were divided into two types: raw (R) and cooked byproduct (C). The proteins were extracted using the pH shift method and quantified using the Bradford assay. It was possible to extract a maximum of 455 mg/g at a neutral pH, for which R had the highest protein yield. Proteins were also qualified using reverse phase high-performance liquid chromatography (RP-HPLC) that showed that R has more hydrophilic proteins while the C extracted protein showed more peaks in the hydrophobic phase. The Fourier-transform infrared spectroscopy (FTIR) indicated the presence of glutamine, tyrosine, and serine in the extracted proteins. Extracted proteins were then hydrolyzed using Alcalase and α-Chymotrypsin. It was possible to obtain higher degrees of hydrolysis (DH) using Alcalase. The hydrolysates were tested for antioxidant activity using the DPPH (2,2-diphenyl-1-picryl-hydrazyl-hydrate) free radical antioxidant assay. Alcalase hydrolysates showed to have overall lower IC50 for stabilization of the DPPH radical than α-Chymotrypsin, the lowest one being 13.92±1.57 µg/mL for the Alcalase hydrolyzed neutral proteins. The IC50 results obtained are significantly lower than the ones described in other studies using the same enzymes or other marine species. This can indicate that more heterogenous mixtures of by-product can originate extracted proteins that when hydrolyzed lead to higher radical scavenging activity, thus making shellfish industry by-product a sustainable and valuable source of antioxidant peptides. Keywords: Shellfish; Bioactive peptides; Protein extraction; Protein hydrolysates, Waste management, Nutraceuticals

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Reports on the topic "Protein A 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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2

Shepodd, Timothy J., and Christopher P. Stephens. Development of porous polymer monoliths for reverse-phase chromatography of proteins. Office of Scientific and Technical Information (OSTI), September 2003. http://dx.doi.org/10.2172/918341.

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