Relevant bibliographies by topics / Recombinant proteins Purification

Academic literature on the topic 'Recombinant proteins Purification'

Author: Grafiati
Published: 10 December 2022
Last updated: 28 January 2023

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Contents

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Recombinant proteins Purification.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Recombinant proteins Purification"

1

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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Kermasha, 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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Dyr, 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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

FARRELL, 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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Funaba, 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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Rosales, 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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Jamrichová, 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.

Full text
Abstract:
AbstractProduction of recombinant proteins in Escherichia coli expression systems has shown many advantages, as well as disadvantages, especially for biotechnological and other down-stream applications. The choice of an appropriate vector depends on the gene, to be cloned for purification procedures and other analyses. Selection of a suitable production strain plays an important role in the preparation of recombinant proteins. The main criteria for the selection of the host organism are the properties of the recombinant produced protein, its subsequent use and the total amount desired. The most common problems in eukaryotic gene expression and recombinant proteins purification are, for instance, post-translational modifications, formation of disulphide bonds, or inclusion bodies. Obtaining a purified protein is a key step enabling further characterization of its role in the biological system. Moreover, methods of protein purification have been developed in parallel with the discovery of proteins and the need for their studies and applications. After protein purification, and also between the individual purification steps, it is necessary to test protein stability under different conditions over time. Shortly, all the essential points have been briefly discussed, which could be encountered during production and purification of a recombinant protein of interest, especially from eukaryotic source and expressed heterogeneously in prokaryotic production system.
APA, Harvard, Vancouver, ISO, and other styles
8

ASENJO, 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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Sheng, 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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Mahmoodi, 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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Dissertations / Theses on the topic "Recombinant proteins Purification"

1

Rutt, George Clifford. "Purification of recombinant proteins." Thesis, Massachusetts Institute of Technology, 1996. http://hdl.handle.net/1721.1/42614.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Ditsch, Andre (Andre Paul). "Purification of recombinant proteins with magnetic nanoclusters." Thesis, Massachusetts Institute of Technology, 2005. http://hdl.handle.net/1721.1/34160.

Full text
Abstract:
Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Chemical Engineering, 2005.
Includes 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.
APA, Harvard, Vancouver, ISO, and other styles
3

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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Gaztambide, Danielle A. "Production and Purification of Synthetic Minor Ampullate Silk Proteins." DigitalCommons@USU, 2018. https://digitalcommons.usu.edu/etd/7306.

Full text
Abstract:
Spider silks are incredible natural materials that have a wide variety of properties that can rival or outperform even common synthetic materials like Nylon and Kevlar. As nature’s architects, orb-weaving spiders spin seven different silks that are used for very specific roles throughout the spider’s lifecycle. These silks are comprised of proteins called spidroins. Each of these spidroins has evolved to have properties such as strength and/or stretch that make these silks successful and highly adapted in their designated roles in web construction, prey capture and reproduction. This study involves the production of minor ampullate silk by genetically modifying the bacteria Escherichia coli. Minor ampullate is a lesser studied silk that is used for the first spiral of the orb web. This spiral is a template that the spider uses to finish the web and provides stability during the web construction. Minor ampullate silk is strong, however it does not stretch so it may be well-suited for certain applications such as ballistic materials. By producing and purifying different arrangements of minor ampullate silk protein, it is possible to learn how this protein can be expressed without using the spider itself. This investigation sheds light on how deviations in the protein sequence and motif arrangement can produce different properties, which can potentially be used to make new materials.
APA, Harvard, Vancouver, ISO, and other styles
5

Biedendieck, 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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Miozzi, 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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Ramey, 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/.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Riddle, 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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Kavoosi, 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.

Full text
Abstract:
Downstream processing of proteins and other biological products has long been dominated by packed-bed chromatography (Rankin 2003). Despite the generally high cost of the technique, chromatography remains widely used because it offers extraordinarily high resolution under conditions that do not denature or alter the chemistry of the product, an imperative for therapeutic proteins since purity and activity are strict requirements. However, the inability of patients and governments to meet the rising costs of healthcare, particularly the cost of recombinant protein therapeutics, and the sharp increase in competition over the past decade for market share of recombinant-protein based treatments of major illnesses have led to intense downward pressure on the cost of goods, especially for high volume products such as monoclonal antibodies and other recombinant proteins (Morrow 2002). Industry is therefore seeking to develop more cost effective downstream processes, including cheaper and more selective forms of chromatography. Generic affinity chromatography based on affinity-tag technology has the potential to simplify downstream processing by achieving higher yields and purities than conventional modes of chromatography. However, the high cost of current affinity tag technologies, due mainly to the expense of their associated affinity chromatography media, limits their application at production scales. This thesis addresses this problem by reporting on a novel affinity chromatography platform utilizing the family 9 carbohydrate-binding module (CBM9) of xylanase 10A from T. maritima , a new affinity tag that binds to both soluble sugars and insoluble cellulose to permit the highly efficient capture and purification of CBM9-tagged fusion proteins on a very inexpensive cellulose-based affinity media. Development of this technology has required (i) design of a generic CBM9 expression vector for production of chimeric fusions containing an N-terminal CBM9, a linker region containing a suitable processing site at its C-terminus for efficient removal of the affinity tag following affinity purification, and a C-terminal target protein, (ii) development of an effective strategy to design a linker sequence to stably connect the CBM9 tag to the target protein and to permit efficient tag removal through enzyme-catalyzed cleavage, (iii) derivation and validation of a mathematical model to predict binding and elution behavior of CBM9 fusion proteins on a high-capacity cellulose column, (iv) solutions to certain technology scale-up issues, including the synthesis of a mechanically stable stationary phase, and finally, (v) validation of the performance of the technology in terms of product yield, purity and concentration factor. Two bioinformatics-based strategies were developed to successfully identify a linker with improved resistance to endogeneous proteases of the host when compared against the popular poly-glycine based linker. A simple and effective assay was developed to identify the optimal conditions for efficient tag removal post-purification. The technique, based on Luminescence Resonance Energy Transfer (LRET) prescreens a library of linkers and processing enzymes to identify a CBM9-target protein fusion with enhanced processing efficiency. A novel two-zone model (TZM) of pore diffusion is presented to describe the rate of uptake of CBM9 fusion proteins within the stationary phase of the associated affinity chromatography column and thereby provide improved predictions of product breakthrough, including elution behavior from a bacterial lysate feed. Finally, a mechanically stable cellulose-based chromatography media was synthesized to allow preparative-scale purification of recombinant proteins using CBM9. A fixed-effect two-way response surface methodology was used to optimize the concentrations of the two primary reactants, epichlorohydrin and dimethyl sulfoxide (DMSO), required to cross-link the starting material, Perloza(TM) MT100, a compressible cellulose-based chromatography resin. This resulted in a cross-linked affinity chromatography media capable of operating at an order-of-magnitude higher linear velocity than permitted by unmodified MT100. In sharp contrast to MT100, the mechanical stability and purification performance of the cross-linked media are not diminished by scale-up or repeated column use. The results of this thesis thereby provide industry with a ready-made expression vector that can be used to express any target protein as a CBM9 fusion protein and to then inexpensively purify the target recombinant protein at an overall level of performance that is either superior or comparable to current commercially available fusion-tag technologies.
Applied Science, Faculty of
Chemical and Biological Engineering, Department of
Graduate
APA, Harvard, Vancouver, ISO, and other styles
10

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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Books on the topic "Recombinant proteins Purification"

1

1952-, Seetharam Ramnath, and Sharma Satish K. 1951-, eds. Purification and analysis of recombinant proteins. New York: M. Dekker, 1991.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
2

Bose, 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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

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

Find full text
APA, Harvard, Vancouver, ISO, and other styles
4

OHOLO 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.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
5

Bose, Kakoli. Textbook on Cloning, Expression and Purification of Recombinant Proteins. Springer Singapore Pte. Limited, 2021.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
6

Giannone, Richard J., and Andrew B. Dykstra. Protein Affinity Tags: Methods and Protocols. Springer New York, 2016.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
7

White, 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.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
8

Guldhe, Abhishek, Deepti Yadav, and Tukayi Kudanga. Fundamentals of Recombinant Protein Production, Purification and Characterization. Elsevier Science & Technology Books, 2023.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
9

DiCiommo, 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.

Find full text
APA, Harvard, Vancouver, ISO, and other styles

Book chapters on the topic "Recombinant proteins Purification"

1

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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Buyel, 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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Singh, 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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Kadir, 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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Luitjens, 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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Ferrer-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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Singh, 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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Wright, 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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Dutta, 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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Hochuli, 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.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "Recombinant proteins Purification"

1

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.

Full text
Abstract:
Removal of bacterial endotoxins from solutions of recombinant proteins is one of the most important issues in the preparation of highly purified preparations suitable for in vivo use. An optimal technology for obtaining preparations purified from bacterial endotoxins has been proposed using purification of preparations of recombinant nucleases of the CRISPR/CAS system as an example. Efficacy of developed technology was compared with other available methods. Removal of bacterial endotoxins was carried out using Triton X-114 detergent added to a concentration of 1% to a solution containing the recombinant protein. It was shown that the content of bacterial endotoxins in solutions of purified proteins obtained according to the proposed technology is 0.3–1.5 EU/ml.
APA, Harvard, Vancouver, ISO, and other styles
2

Ashok 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.

Full text
Abstract:
Factor IX, a plasma protein, plays a critical role in blood coagulation. The biological activity of factor IX as well as several other plasma proteins depends on the presence of gamma-carboxy glutamic acid (Gla) residues in their amino terminal region. In vitro mutagenesis has been used to selectively replace Gla residues of factor IX with aspartic acid (Asp) residues in order to establish the contribution of individual as well as paired Gla residues to the normal functioning of the protein. These substitutions were made at positions 7, 15, 20 and 26 in human factor IX. In addition, residue number 18, a cysteine has been changed to serine in an attempt to disrupt the highly conserved disulfide bond in the gla-domain. The gla-domain mutants will be produced in mammalian cells and compared with native recombinant factor IX. A rapid immunoaffinity purification procedure, which has been used to obtain recombinant factor IX produced in the presence or absence of vitamin K, is being used to purify the mutants. Protein sequence analysis has been used to confirm complete processing and proper gamma-carboxylation of recombinant factor IX. The properties of these mutants as compared to human factor IX will be discussed.
APA, Harvard, Vancouver, ISO, and other styles
3

Karges, 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.

Full text
Abstract:
Isolation and purification of antithrombin III (AT III) by affinity chromatography on immobilized heparin is a standard method for the large scale preparation of this protein from human or animal plasma. Hence, after AT III became available by gentechnological methods, we tried to adapt this procedure for the isolation of AT III from supernatants of mammalian- and yeast-cells. Indeed, it was possible to use this method also for the isolation of the recombinant gene products. Since, however, the cell growth media contain heterologous protein or peptide mixtures like fetal calf serum, the method had to be improved to avoid the adsorption of non human proteins or peptides. We are now able to purify AT III from CHO-cell-superna-tants to more than 95 % purity. The characterization of this AT III-product by double immuno diffusion revealed that it is immunologically totally identical with the authentic material from plasma. AT III antigen content, progressive inhibitor activity and heparin cofactor activity compare very well in the final product; hence, it is totally active compared to AT III from plasma.In polyacrylamidegel electrophoresis most of the material migrated differently to the authentic material showing 9 bands in equal distance to each other, instead four in the At III from plasma. After degradation with sialinidase from both AT III preparations identical cleavage products were obtained migrating predominantly as a single band. Hence, the electrophoretic heterogeneity seems to be due to a different degree of sialinyla-tion of the products.
APA, Harvard, Vancouver, ISO, and other styles
4

Mitra, 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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Gheysen, 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.

Full text
Abstract:
A hybrid between human tissue-type plasminogen activator (t-PA) and human single chain urokinase-type plasminogen activator (scu-PA) was obtained by ligation of cDNA fragments encoding the NH2-terminal amino acids 1 to 67 of t-PA and the COOH-ter-minal amino acids 136 to 411, of scu-PA. Both this chimaeric cDNA and cDNA encoding scu-PA were expressed in a mammalian system (HAK-cells) using bovine papilloma virus (BPV) derived vectors. Two stable cell lines were obtained which secreted the recombinant hybrid and the scu-PA at 1 μg/ml and 2 μg/ml u-PA related antigen respectively into the culture medium. Following purification by Zinc chelate Sepharose, immunoadsorption chromatography, benzamidine-Sepharose and Ultrogel AcA44 gel filtration, highly purified proteins were obtained with a yield of about 200 μg/1. SDS gel electrophoresis under reducing conditions showed single bands with M 43,000 and M 50,000 respectively. Following conversion to urokinase with plasmin, both proteins had a specific amidolytic activity comparable to that of natural scu-PA. Both proteins activated plasminogen directly with km1.4 and 0.5 μM and k2 0.0034 s and 0.0027 s . Neither protein bound specifically to fibrin.Thus the fusion of the finger-like domain of t-PA to the COOH-terminal part of scu-PA does not confer fibrin affinity of t-PA to this chimaeric protein. However, peptide material can be fused to the COOH-terminal part of scu-PA without perturbing its enzymatic properties.
APA, Harvard, Vancouver, ISO, and other styles
6

Nurjayadi, 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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Vermeer, 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.

Full text
Abstract:
In vivo treatment of experimental animals with vitamin K-antagonists induces the accumulation of non-carboxylated coagulation factor precursors in the liver, where they are tightly bound to vitamin K-dependent carboxylase. If hepatic carboxylase is isolated from warfarin-treated animals, it is obtained therefore almost exclusively in the form of an enzyme/substrate complex. If carboxylase is prepared from non-treated animals, on the other hand, the resulting enzyme is predominantly substrate-free. Small substrates like F L E E L or decarboxylated osteocalcinare carboxylated equally well by both types of carboxylase, but protein substrates(Mr > 30 000) are recognized exclusively by substrate-free carboxylase.Initial attempts to purify carboxylasewere performed with livers from warfarin-treated cows as a starting material. Antibodies against the normal blood coagulation factors crossreact with the hepatic precursor proteins so that the enzyme/substrate complexes could be specifically extracted from detergent-solubilized microsomes by the substrate/antibody interaction. This procedure resulted ina substantial purification of carboxylase, but because its endogenous substrate remained firmly bound, even after it had been carboxylated in vitro, the enzyme system was not suitable for the carboxylation of protein substrates.Therefore a second strategy was developed by which substrate-free carboxylase (from normal livers) was partly purified by sequential extraction of the microsomal membranes with detergents, followed by ammonium sulfate precipitation and size exclusion chromatography.This procedure resulted in a soluble carboxylase complex, still consisting of 7 proteins and phosphatidylcholine. Although further dissociation of the complex resulted in a complete loss of activity, it is not sure if all components play a role in the carboxylation reaction. Exogenous substrates which could be carboxylated by substrate-free carboxylase were: the penta-peptide F L E E L, descarboxyprothrombin from bovine plasma, thermally decarboxylated osteocalcin from bovine bone and non-car-boxy lated coagulaton factor precursors which had been produced by recombinant-DNA techniques in various laboratories. The . efficiency of CO^ incorporation was: 1 mole per 100 moles of F L E E L, 1 mole per 240 moles of descarboxy-prothrombin, 1 mole per mole of decarboxylated osteocalcin and 8 moles per mole of a recombinant factor IX precursor. We assume that the high efficiency with which the recombinant coagulation factor precursors were carboxylated is due to the presence of at least part of their leader sequence. The importance of the aminoacid chain preceding the first carboxylatable Glu residue is demonstrated by the fact that descarboxylated osteocalcin of bovine origin is carboxylated with a relatively high efficiency, whereas descarboxylated osteocalcin from monkey bone is not recognized atal.. Yet the only difference between the two substrates is found in their aminoacids 3 and 4, whereas the first carboxylatable Glu occurs at position 17. It seems, therefore, that the aminoacids 1-16 in bovine osteocalcin mimic to some extent part of the leader sequence in the coagulation factor precursors. Chemical or biochemical modification of decarboxylated osteocalcin might reveal which structural features contribute to its recognition by hepatic carboxylase.The optimal conditions for carboxylation include a high concentration of dithiols (e.g. DTT) and under these conditions disulfide bridges are reduced. Obviously this will lead to a complete destruction of the biological activity of various carboxylated products. Therefore we have searched for a more natural reducing system and it was found that the bacterial thioredoxin/thiore-doxin-reductase system in the presence of 40 uM NADFH was able to replace DTT in the reaction mixtures. Since a comparable system also occurs in calf liver it seems not unlikely that this is the physiological counterpart of the dithiols used in vitro.
APA, Harvard, Vancouver, ISO, and other styles
8

Smith, 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.

Full text
Abstract:
Commercial concentrates (CC) of vitamin K dependent coagulation factors may cause thrombosis or coagulation factor consumption while more highly purified (17 U/mg) factor IX (IX) concentrates do not seem to be thrombogenic (Menache et al, Blood 64:1220, 1984). Monoclonal antibody (MAb) immunoaffinity purified IX of high specific activity from CC or recombinant factor IX sources may also improve therapy. In this report, 400 mg of Affigel-10 linked A-7 MAb was used to bind factor IX in the presence of metal ions (20 mM MgCl2). Elution of IX was with 20 mM EDTA. Thrombogenicity of CC and IX prepared from CC by MAb immunoaffinity was tested. A CC which was thrombogenic in the stasis thrombosis assay (CC #1) produced large thrombi at doses of 50, 50, and 100 U/kg while none were seen with the IX produced from this CC at doses of 106 and 234 U/kg. A heparin treated CC (CC #2) which was not thrombogenic in the stasis-thrombosis assay at doses of 100 U/kg was infused in 4 rabbits at 100 U/kg and platelets, fibrinogen, AT-III antigen, and factors IX, V, and VIII were monitored for 5 hours post-infusion. Immunoaffinity IX from this CC was infused in 4 rabbits at 214-243 U/kg for comparison. Mean platelet count decrease was 20% in CC group and 8% for the IX group. Mean factor V and VIII decreased 26 and 36% respectively with CC while no decrease was seen in the IX rabbits (p < .05). Fibrinogen values and AT-III did not differ for IX or CC groups. Mean factor IX activity at 1 hour increased 1.6 fold for CC and 3 fold for IX. Yields for IX purification were 80 and 85%. Clotting activity was 143 and 101 U/mg and antigen was approximately 200 U/mg. Purification was over 90 fold by MAb immunoaf f inity. There was no detectable factor II, VII or X activity in MAb purified IX. Non-activated PTT was greater than 200 seconds for CC #1 and 158 seconds for CC #2. Column capacity was at least 150 mg. These results demonstrate that factor IX is not the thrombogenic component of some CC. Also, IX prepared by MAb immunoaffinity may have therapeutic advantage for patients at risk for thrombosis and adverse effects of contaminating proteins in commercial concentrates.
APA, Harvard, Vancouver, ISO, and other styles
9

Yuan, 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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Wiratama, 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.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Reports on the topic "Recombinant proteins Purification"

1

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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Palmer, 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.

Full text
Abstract:
Anaplasmosis is an arthropod+borne disease of cattle caused by the rickettsia Anaplasma marginale and an impediment to efficient production of healthy livestock in both Israel and the United States. Our research focuses on development of a recombinant membrane surface protein (MSP) immunogen to replace current vaccines derived from the blood of infected cattle. The risk of widespread transmission of both known and newly emergent pathogens has prevented licensure of live blood-based vaccines in the U.S. and is a major concern for their continued use in Israel. Briefly, we accomplished the following in our BARD supported research: i) characterization of the intramolecular and intermolecular relationships of the native Major Surface Proteins (MSP) in the outer membrane; ii) expression, purification, and epitope characterization of the recombinant MSP-2, MSP-3, MSP-4, and MSP-5 proteins required to construct the recombinant ISCOM; iii) demonstration that the outer membrane-Quil A induces CD4+ T lymphocytes specific for the outer membrane polypeptides; iv) identification of CD4+ T lymphocytes that recognize outer membrane polypeptide epitopes conserved among other wise antigenically distinct strains; v) determination that immunization with the outer membrane-Quil A construct does not affect the ability of ticks to acquire or transmit A. marginale; and vi) demonstration that the outer membrane-Quil A construct induces complete protection against rickettsemia upon homologous challenge and significant protection against challenge with antigenically distinct strains, including tick transmission. Importantly, the level of protection against homologous challenge in the MSP vaccinates was comparable to that induced by live blood-based vaccines and demonstrates that development of a new generation of vaccines is feasible.
APA, Harvard, Vancouver, ISO, and other styles
3

Chan, 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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'Recombinant proteins Purification' for particular source types:
Journal articles Dissertations / Theses
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography