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Статті в журналах з теми "Recombinant proteins Purification"
Southan, Christopher. "Purification and analysis of recombinant proteins." Trends in Biotechnology 10 (1992): 226. http://dx.doi.org/10.1016/0167-7799(92)90226-l.
Повний текст джерелаKermasha, S., and I. Alli. "Purification and analysis of recombinant proteins." Food Research International 26, no. 2 (January 1993): 158–59. http://dx.doi.org/10.1016/0963-9969(93)90072-q.
Повний текст джерелаDyr, J. Evangelista, and J. Suttnar. "Separation used for purification of recombinant proteins." Journal of Chromatography B: Biomedical Sciences and Applications 699, no. 1-2 (October 1997): 383–401. http://dx.doi.org/10.1016/s0378-4347(97)00201-6.
Повний текст джерелаFARRELL, DECLAN J. "Purification of recombinant proteins for pharmaceutical use." Biochemical Society Transactions 18, no. 2 (April 1, 1990): 243–45. http://dx.doi.org/10.1042/bst0180243.
Повний текст джерелаFunaba, Masayuki, and Lawrence S. Mathews. "Recombinant Expression and Purification of Smad Proteins." Protein Expression and Purification 20, no. 3 (December 2000): 507–13. http://dx.doi.org/10.1006/prep.2000.1315.
Повний текст джерелаRosales, Jesusa L., and Ki-Young Lee. "Purification of Dual-Tagged Intact Recombinant Proteins." Biochemical and Biophysical Research Communications 273, no. 3 (July 2000): 1058–62. http://dx.doi.org/10.1006/bbrc.2000.3063.
Повний текст джерелаJamrichová, Daniela, Lenka Tišáková, Veronika Jarábková, and Andrej Godány. "How to approach heterogeneous protein expression for biotechnological use: An overview." Nova Biotechnologica et Chimica 16, no. 1 (June 27, 2017): 1–11. http://dx.doi.org/10.1515/nbec-2017-0001.
Повний текст джерелаASENJO, J. A., J. PARRADO, and B. A. ANDREWS. "Rational Design of Purification Processes for Recombinant Proteins." Annals of the New York Academy of Sciences 646, no. 1 Recombinant D (December 1991): 334–56. http://dx.doi.org/10.1111/j.1749-6632.1991.tb18596.x.
Повний текст джерелаSheng, S., P. A. Pemberton, and R. Sager. "Production, purification, and characterization of recombinant maspin proteins." Journal of Biological Chemistry 269, no. 49 (December 1994): 30988–93. http://dx.doi.org/10.1016/s0021-9258(18)47379-6.
Повний текст джерелаMahmoodi, Sahar, Mohammad Pourhassan-Moghaddam, David W. Wood, Hasan Majdi, and Nosratollah Zarghami. "Current affinity approaches for purification of recombinant proteins." Cogent Biology 5, no. 1 (January 1, 2019): 1665406. http://dx.doi.org/10.1080/23312025.2019.1665406.
Повний текст джерелаДисертації з теми "Recombinant proteins Purification"
Rutt, George Clifford. "Purification of recombinant proteins." Thesis, Massachusetts Institute of Technology, 1996. http://hdl.handle.net/1721.1/42614.
Повний текст джерелаDitsch, Andre (Andre Paul). "Purification of recombinant proteins with magnetic nanoclusters." Thesis, Massachusetts Institute of Technology, 2005. http://hdl.handle.net/1721.1/34160.
Повний текст джерелаIncludes bibliographical references.
This thesis focused on the development and analysis of a new class of magnetic fluids for recovery of recombinant proteins from fermentation broth. Magnetic fluids are colloidally stable dispersions of magnetic nanoclusters in water that do not settle gravitational and moderate magnetic fields due to their small size. The magnetic nanoclusters possess large surface area for protein adsorption without any porous structure, resulting in much faster mass transfer than in traditional separations. The magnetic nanoclusters consist of 25-200 nm clusters of 8 nm magnetite (Fe₃0₄) cores coated with poly(acrylic acid-co-styrenesulfonic acid-co-vinylsulfonic acid). For use in separation, clusters must be recoverable from solution. Individual nanoparticles are too small to be recovered efficiently, while 50nm or larger clusters of primary particles are easily recovered. Cluster size depends on polymer molecular weight and hydrophobicity as well as the amount of polymer present at nucleation. When a polymer coating with optimal molecular weight is used in limited amounts, clusters are formed. When the clusters are subsequently coated with additional polymer, the clusters are stable in high ionic strength environments (>5M NaCl), while retaining the necessary cluster size for efficient magnetic recovery.
(cont.) Models have been developed to predict the optimal molecular weight, and the cluster size obtained with limited amounts of polymer or polymers other than the optimal molecular weight. The models and methods have been verified with other polymer coatings, indicating that the methods can be used to synthesize a wide range of stable nanoclusters. Due to rapid mass transfer, the rate-limiting step of the purification scheme is recovery of the nanoclusters from solution with high gradient magnetic separation (HGMS). The nanoclusters can be recovered extremely efficiently, up to 99.9% at high flow rates, up to 10,000 cm/hr. A detailed model of HGMS has been developed to quantitatively predict capture, and simpler methods have been developed to predict the maximum capture and capacity of the column without computationally expensive simulations. The use of the nanoclusters for protein purification was studied both with model proteins the recombinant protein drosomycin from Pichia pastoris fermentation broth. The nanoclusters have high adsorptive capacities of up to 900 mg protein/mL adsorbent, nearly an order of magnitude higher than the best commercially available porous adsorbents. Adsorption can be performed both by ion exchange and hydrophobic interactions, allowing nearly pure drosomycin to be recovered from clarified fermentation broth in a single step.
(cont.) When used in whole cell broth, the nanoclusters bind to proteins on the surface of the Pichia pastoris cells at conditions where drosomycin is bound, limiting the effectiveness of the separation. When proteins are bound at conditions where nanoclusters do not bind to cells, cell clarification and protein purification can be performed in one fast step. A simple model of the cell binding has been developed, providing guidelines for use of magnetic nanoparticles in the presence of cells.
by Andre Ditsch.
Ph.D.
Lee, Jae-Yong. "Expression, purification and interaction analysis of recombinant SRB proteins." Thesis, Imperial College London, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.407809.
Повний текст джерелаGaztambide, Danielle A. "Production and Purification of Synthetic Minor Ampullate Silk Proteins." DigitalCommons@USU, 2018. https://digitalcommons.usu.edu/etd/7306.
Повний текст джерелаBiedendieck, Rebekka Katrin Johanna. "Bacillus megaterium versatile tools for production, secretion and purification of recombinant proteins /." kostenfrei, 2007. http://www.digibib.tu-bs.de/?docid=00018998.
Повний текст джерелаMiozzi, Jackelyn. "Column-free Purification Method for Recombinant Proteins Using a Self-Cleaving Aggregating tag." The Ohio State University, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=osu15229401048581.
Повний текст джерелаRamey, Aaron Thomson. "Optimizing production methods for artificial silk proteins through bioreactor and purification studies of recombinant proteins expressed from Pichia pastoris." Connect to this title online, 2006. http://etd.lib.clemson.edu/documents/1175185569/.
Повний текст джерелаRiddle, Suzette Renee. "Purification and characterization of two recombinant proteins: Annexin III and phosphatidyl inositol specific-phospholipase C /." The Ohio State University, 1997. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487943610782957.
Повний текст джерелаKavoosi, Mojgan. "The CBM9 fusion tag : a new technology for inexpensive production and affinity purification of recombinant proteins." Thesis, University of British Columbia, 2007. http://hdl.handle.net/2429/31363.
Повний текст джерелаApplied Science, Faculty of
Chemical and Biological Engineering, Department of
Graduate
Bandmann, Nina. "Rational and combinatorial genetic engineering approaches for improved recombinant protein production and purification." Doctoral thesis, Stockholm : Bioteknologi, Kungliga Tekniska högskolan, 2007. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-4318.
Повний текст джерелаКниги з теми "Recombinant proteins Purification"
1952-, Seetharam Ramnath, and Sharma Satish K. 1951-, eds. Purification and analysis of recombinant proteins. New York: M. Dekker, 1991.
Знайти повний текст джерелаBose, Kakoli, ed. Textbook on Cloning, Expression and Purification of Recombinant Proteins. Singapore: Springer Singapore, 2022. http://dx.doi.org/10.1007/978-981-16-4987-5.
Повний текст джерелаProtein affinity tags: Methods and protocols. New York: Humana Press, 2014.
Знайти повний текст джерелаOHOLO Conference (35th 1990 Elat, Israel). Biologicals from recombinant microorganisms and animal cells: Production and recovery : proceedings of the 34th [i.e. 35th] Oholo Conference, Eilat, Israel, 1990. Rehovot, Israel: Balaban Publishers, 1991.
Знайти повний текст джерелаBose, Kakoli. Textbook on Cloning, Expression and Purification of Recombinant Proteins. Springer Singapore Pte. Limited, 2021.
Знайти повний текст джерелаGiannone, Richard J., and Andrew B. Dykstra. Protein Affinity Tags: Methods and Protocols. Springer New York, 2016.
Знайти повний текст джерелаWhite, M. D., and S. Reuveny. Biologicals from Recombinant Microorganisms and Animal Cells: Production and Recovery : Proceedings of the 34th Oholo Conference, Eilat, Israel, 1990 (Oholo Conference//Proceedings). Vch Pub, 1991.
Знайти повний текст джерелаGuldhe, Abhishek, Deepti Yadav, and Tukayi Kudanga. Fundamentals of Recombinant Protein Production, Purification and Characterization. Elsevier Science & Technology Books, 2023.
Знайти повний текст джерелаDiCiommo, David P. A novel, DNA-based alphavirus gene expression system for rapid recombinant protein purification and virus-based gene delivery to retina and retinoblastoma tumor cells. 2002.
Знайти повний текст джерелаЧастини книг з теми "Recombinant proteins Purification"
Acharya, Saujanya, Roshnee Bose, and Kakoli Bose. "Purification of Difficult Proteins." In Textbook on Cloning, Expression and Purification of Recombinant Proteins, 249–78. Singapore: Springer Singapore, 2022. http://dx.doi.org/10.1007/978-981-16-4987-5_10.
Повний текст джерелаBuyel, Johannes F. "Strategies for Efficient and Sustainable Protein Extraction and Purification from Plant Tissues." In Recombinant Proteins in Plants, 127–45. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2241-4_9.
Повний текст джерелаSingh, Nitu, and Kakoli Bose. "Introduction to Recombinant Protein Purification." In Textbook on Cloning, Expression and Purification of Recombinant Proteins, 115–40. Singapore: Springer Singapore, 2022. http://dx.doi.org/10.1007/978-981-16-4987-5_5.
Повний текст джерелаKadir, Farida, Paul Ives, Alfred Luitjens, and Emile van Corven. "Production and Purification of Recombinant Proteins." In Pharmaceutical Biotechnology, 47–67. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-6486-0_3.
Повний текст джерелаLuitjens, Alfred, and Emile van Corven. "Production and Purification of Recombinant Proteins." In Pharmaceutical Biotechnology, 57–82. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-00710-2_4.
Повний текст джерелаFerrer-Miralles, Neus, Paolo Saccardo, José Luis Corchero, and Elena Garcia-Fruitós. "Recombinant Protein Production and Purification of Insoluble Proteins." In Methods in Molecular Biology, 1–31. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-1859-2_1.
Повний текст джерелаSingh, N. Dolendro, Yi Ding, and Henry Daniell. "Chloroplast-Derived Vaccine Antigens and Biopharmaceuticals: Protocols for Expression, Purification, or Oral Delivery and Functional Evaluation." In Recombinant Proteins From Plants, 163–92. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-59745-407-0_10.
Повний текст джерелаWright, Gordon, and Alan Colman. "Purification of Recombinant Proteins from Sheep's Milk." In Transgenic Animals, 469–71. London: CRC Press, 2022. http://dx.doi.org/10.1201/9781003211099-85.
Повний текст джерелаDutta, Shubhankar, and Kakoli Bose. "Protein Purification by Affinity Chromatography." In Textbook on Cloning, Expression and Purification of Recombinant Proteins, 141–71. Singapore: Springer Singapore, 2022. http://dx.doi.org/10.1007/978-981-16-4987-5_6.
Повний текст джерелаHochuli, Erich. "Purification of Recombinant Proteins with Metal Chelate Adsorbent." In Genetic Engineering, 87–98. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4613-0641-2_6.
Повний текст джерелаТези доповідей конференцій з теми "Recombinant proteins Purification"
Tyumentsev, A. I., M. A. Tyumentseva, and V. G. Akimkin. "DEVELOPMENT OF APPROACHES FOR ENDOTOXIN REMOVAL FROM PROTEIN PREPARATIONS ON THE EXAMPLE OF NUCLEASES OF THE CRISPR/CAS SYSTEM." In Molecular Diagnostics and Biosafety. Federal Budget Institute of Science 'Central Research Institute for Epidemiology', 2020. http://dx.doi.org/10.36233/978-5-9900432-9-9-113.
Повний текст джерелаAshok Kumar, A., Margaret Insley, Jay Gambee, Sharon J. Busby, and Kathleen L. Berkner. "SITE SPECIFIC MUTAGENESIS WITHIN THE GLA-DOMAIN OF HUMAN FACTOR IX." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644079.
Повний текст джерелаKarges, H. E., G. Zettlemeiβl, H. Naumann, U. Eberhard, and M. Bröker. "PURIFICATION AND CHARACTERIZATION OF GENTECHNOLOGICALLY PREPARED ANTITHROMBIN III." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643684.
Повний текст джерелаMitra, Sayantan, Mike Vierra, Boris Levitan, Gia Jokadze, and Andrew Farmer. "Abstract B129: Novel miniprep system for rapid purification of recombinant proteins and antibodies on high capacity membranes." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics; November 5-9, 2015; Boston, MA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1535-7163.targ-15-b129.
Повний текст джерелаGheysen, D., L. Piérard, P. Jacobs, H. R. Lijnen, A. Bollen, and D. Collen. "PROPERTIES OF A HUMAN RECOMBINANT FUSION PROTEIN OF THE ‘FINGER’ DOMAIN OF TISSUE-TYPE PLASMINOGEN ACTIVATOR (t-PA) AND A TRUNCATED SINGLE CHAIN UROKINASE-TYPE PLASMINOGEN ACTIVATOR (scu-PA)." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643941.
Повний текст джерелаNurjayadi, M., H. Setyo, D. Hardianto, K. Agustini, and H. Ali El-Enshasy. "Purification of Salmonella Typhi Fim-C recombinant proteins with Co-NTA resins as raw materials for development of rapid typhoid fever detection kit." In THE 2ND SCIENCE AND MATHEMATICS INTERNATIONAL CONFERENCE (SMIC 2020): Transforming Research and Education of Science and Mathematics in the Digital Age. AIP Publishing, 2021. http://dx.doi.org/10.1063/5.0041890.
Повний текст джерелаVermeer, C., BA M. Soute, and MM W. Ulrich. "IN VITRO CARBOXYLATION OF EXOGENOUS PROTEIN SUBSTRATES BY VITAMIN K-DEPENDENT CARBOXYLASE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643994.
Повний текст джерелаSmith, K. J. "INFUSION OF MONOCLONAL ANTIBODY IMMUNOAFFINITY PURIFIED FACTOR IX IN RABBITS: COMPARISON WITH COMMERCIAL CONCENTRATES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644066.
Повний текст джерелаYuan, Mengru, Yongping Jiang, and Wei Dai. "Abstract 457: Expression, purification, and characterization of recombinant TAT-SALL4B protein." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-457.
Повний текст джерелаWiratama, Ihsan, Heri Hermansyah, Anondho Wijarnako, Amarila Malik, Raditya Imamul Khalid, and Muhamad Sahlan. "Purification of recombinant protein apoptin from two cell host Bacillus subtilis 168 and Escherichia coli Bl21 Star™." In SECOND INTERNATIONAL CONFERENCE OF MATHEMATICS (SICME2019). Author(s), 2019. http://dx.doi.org/10.1063/1.5096732.
Повний текст джерелаЗвіти організацій з теми "Recombinant proteins Purification"
Adams, Michael W., and Michael W. W. Adams. MAGGIE Component 1: Identification and Purification of Native and Recombinant Multiprotein Complexes and Modified Proteins from Pyrococcus furiosus. Office of Scientific and Technical Information (OSTI), January 2014. http://dx.doi.org/10.2172/1113776.
Повний текст джерелаPalmer, Guy H., Eugene Pipano, Terry F. McElwain, Varda Shkap, and Donald P. Knowles, Jr. Development of a Multivalent ISCOM Vaccine against Anaplasmosis. United States Department of Agriculture, July 1993. http://dx.doi.org/10.32747/1993.7568763.bard.
Повний текст джерелаChan, Eva. Expression and Purification of Recombinant Protein to Generate a Monoclonal Antibody to the PX domain of Tks5 ? Isoform in Cancer Cells. Portland State University Library, January 2016. http://dx.doi.org/10.15760/honors.323.
Повний текст джерела