Journal articles: '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.

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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.

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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.

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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.

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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.

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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.

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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.

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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.

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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.

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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.

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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.

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11

Leser, E. W., and J. A. Asenjo. "Rational design of purification processes for recombinant proteins." Journal of Chromatography B: Biomedical Sciences and Applications 584, no. 1 (December 1992): 43–57. http://dx.doi.org/10.1016/0378-4347(92)80008-e.

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12

Wilken, Lisa R., and Zivko L. Nikolov. "Recovery and purification of plant-made recombinant proteins." Biotechnology Advances 30, no. 2 (March 2012): 419–33. http://dx.doi.org/10.1016/j.biotechadv.2011.07.020.

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13

Tripathi, Nagesh K. "Production and Purification of Recombinant Proteins fromEscherichia coli." ChemBioEng Reviews 3, no. 3 (May 12, 2016): 116–33. http://dx.doi.org/10.1002/cben.201600002.

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14

Levourch, Gaëlle, Noureddine Lebaz, and Abdelhamid Elaissari. "Hydrophilic Submicron Nanogel Particles for Specific Recombinant Proteins Extraction and Purification." Polymers 12, no. 6 (June 24, 2020): 1413. http://dx.doi.org/10.3390/polym12061413.

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In biomedical diagnosis and bionanotechnologies, the extraction and purification of proteins and protein derivatives are of great interest. In fact, to purify recombinant proteins for instance, new methodologies and well appropriate material supports need to be established and also to be evaluated. In this work, hydrophilic nanohydrogel particles were prepared for recombinant proteins extraction for purification purpose. The prepared nanohydrogel polymer-based particles are hydrophilic below the volume phase transition temperature (TVPT) and dehydrated above the TVPT, due to the thermally sensitive poly(N-alkyl acrylamide) and poly(N-alkyl methacrylamide) derivatives. Then, the use of heavy metal ions in the presence of such functional particles should specifically capture recombinant proteins (i.e., proteins bearing a poly(histidine) part). In order to understand and to optimize the specific capture and the purification of recombinant proteins, various parameters have been investigated as a systematic study. Firstly, the adsorption was investigated as a function of pH and protein concentration. According to high hydration of the prepared nanohydrogel, no marked adsorption was observed. Secondly, the effect of pH was investigated and found to be the driven parameter affecting the metal ions immobilization and the recombinant proteins complexation. As a result, high protein complexation was observed at basic pH compared to non-complexation at acidic pH medium. The immobilized proteins via complexation were released by changing the pH. This decomplexation seems to be effective but depends on fixation conditions and particle surface structure.

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Jerlström-Hultqvist, Jon, Britta Stadelmann, Sandra Birkestedt, Ulf Hellman, and Staffan G. Svärd. "Plasmid Vectors for Proteomic Analyses in Giardia: Purification of Virulence Factors and Analysis of the Proteasome." Eukaryotic Cell 11, no. 7 (May 18, 2012): 864–73. http://dx.doi.org/10.1128/ec.00092-12.

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ABSTRACTIn recent years, proteomics has come of age with the development of efficient tools for purification, identification, and characterization of gene products predicted by genome projects. The intestinal protozoanGiardia intestinaliscan be transfected, but there is only a limited set of vectors available, and most of them are not user friendly. This work delineates the construction of a suite of cassette-based expression vectors for use inGiardia. Expression is provided by the strong constitutive ornithine carbamoyltransferase (OCT) promoter, and tagging is possible in both N- and C-terminal configurations. Taken together, the vectors are capable of providing protein localization and production of recombinant proteins, followed by efficient purification by a novel affinity tag combination, streptavidin binding peptide–glutathioneS-transferase (SBP-GST). The option of removing the tags from purified proteins was provided by the inclusion of a PreScission protease site. The efficiency and feasibility of producing and purifying endogenous recombinantGiardiaproteins with the developed vectors was demonstrated by the purification of active recombinant arginine deiminase (ADI) and OCT from stably transfected trophozoites. Moreover, we describe the tagging, purification by StrepTactin affinity chromatography, and compositional analysis by mass spectrometry of theG. intestinalis26S proteasome by employing the Strep II-FLAG–tandem affinity purification (SF-TAP) tag. This is the first report of efficient production and purification of recombinant proteins in and fromGiardia, which will allow the study of specific parasite proteins and protein complexes.

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Heijbel, A., K. Andersson, M. Carlsson, and C. Gustafsson. "Purification of Poly(His)-tagged Recombinant Proteins using HisTrap." Biochemical Society Transactions 28, no. 5 (October 1, 2000): A261. http://dx.doi.org/10.1042/bst028a261a.

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17

Mello, Charlene M., Jason W. Soares, Steven Arcidiacono, and Michelle M. Butler. "Acid Extraction and Purification of Recombinant Spider Silk Proteins." Biomacromolecules 5, no. 5 (September 2004): 1849–52. http://dx.doi.org/10.1021/bm049815g.

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18

Airenne, Kari J., and Markku S. Kulomaa. "Rapid purification of recombinant proteins fused to chicken avidin." Gene 167, no. 1-2 (December 1995): 63–68. http://dx.doi.org/10.1016/0378-1119(95)00631-1.

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19

Harris, Jeffrey D., Christopher A. Seid, Gregory K. Fontenot, and Hui F. Liu. "Expression and Purification of Recombinant Human Zona Pellucida Proteins." Protein Expression and Purification 16, no. 2 (July 1999): 298–307. http://dx.doi.org/10.1006/prep.1999.1060.

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Desai, Urvee A., Gargi Sur, Sylvia Daunert, Ruth Babbitt, and Qingshun Li. "Expression and Affinity Purification of Recombinant Proteins from Plants." Protein Expression and Purification 25, no. 1 (June 2002): 195–202. http://dx.doi.org/10.1006/prep.2002.1627.

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Saraswat, Mayank, Luca Musante, Alessandra Ravidá, Brian Shortt, Barry Byrne, and Harry Holthofer. "Preparative Purification of Recombinant Proteins: Current Status and Future Trends." BioMed Research International 2013 (2013): 1–18. http://dx.doi.org/10.1155/2013/312709.

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Advances in fermentation technologies have resulted in the production of increased yields of proteins of economic, biopharmaceutical, and medicinal importance. Consequently, there is an absolute requirement for the development of rapid, cost-effective methodologies which facilitate the purification of such products in the absence of contaminants, such as superfluous proteins and endotoxins. Here, we provide a comprehensive overview of a selection of key purification methodologies currently being applied in both academic and industrial settings and discuss how innovative and effective protocols such as aqueous two-phase partitioning, membrane chromatography, and high-performance tangential flow filtration may be applied independently of or in conjunction with more traditional protocols for downstream processing applications.

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22

Ryu, Jaewook, Ukjin Lee, Jiye Park, Do-Hyun Yoo, and Jung Hoon Ahn. "A Vector System for ABC Transporter-Mediated Secretion and Purification of Recombinant Proteins in Pseudomonas Species." Applied and Environmental Microbiology 81, no. 5 (December 29, 2014): 1744–53. http://dx.doi.org/10.1128/aem.03514-14.

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ABSTRACTPseudomonas fluorescensis an efficient platform for recombinant protein production.P. fluorescenshas an ABC transporter secreting endogenous thermostable lipase (TliA) and protease, which can be exploited to transport recombinant proteins across the cell membrane. In this study, the expression vector pDART was constructed by insertingtliDEF, genes encoding the ABC transporter, along with the construct of the lipase ABC transporter recognition domain (LARD), into pDSK519, a widely used shuttle vector. When the gene for the target protein was inserted into the vector, the C-terminally fused LARD allowed it to be secreted through the ABC transporter into the extracellular medium. After secretion of the fused target protein, the LARD containing a hydrophobic C terminus enabled its purification through hydrophobic interaction chromatography (HIC) using a methyl-Sepharose column. Alkaline phosphatase (AP) and green fluorescent protein (GFP) were used to validate the expression, export, and purification of target proteins by the pDART system. Both proteins were secreted into the extracellular medium inP. fluorescens. In particular, AP was secreted in severalPseudomonasspecies with its enzymatic activity in extracellular media. Furthermore, purification of the target protein using HIC yielded some degree of AP and GFP purification, where AP was purified to almost a single product. The pDART system will provide greater convenience for the secretory production and purification of recombinant proteins in Gram-negative bacteria, such asPseudomonasspecies.

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23

Kit, M. Yu. "Development of recombinant antigen expression and purification for African swine fever serological diagnostics." Journal for Veterinary Medicine, Biotechnology and Biosafety 7, no. 3 (September 28, 2021): 24–31. http://dx.doi.org/10.36016/jvmbbs-2021-7-3-4.

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The paper reports the purification and its optimization of recombinant proteins p10, p32, p54, p54ΔTM, DNA ligase and DNA ligaseΔDBD of African swine fever virus. The corresponding coding sequences were subcloned into pASG-IBA105 and pASG-IBA103 vectors, multiplied and used for transformation of competent E. coli expression strain. Expressed proteins were purified using Strep-Tactin XT purification system under native and denaturing conditions, as well as using detergents according to the optimized protocol for recombinant proteins solubilization from inclusion bodies. Among all expressed and purified proteins p32 and p54 were found to be immunoreactive and specific. Although p54 was unstable during long-term storage, after further storage condition optimization, the protein can be used for indirect ASF ELISA development. Recombinant p32 was shown to be an effective antigen for ASF ELISA providing detection of antibodies against ASFV with low background signal

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24

Leong, Louis E. C. "The Use of Recombinant Fusion Proteases in the Affinity Purification of Recombinant Proteins." Molecular Biotechnology 12, no. 3 (1999): 269–74. http://dx.doi.org/10.1385/mb:12:3:269.

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25

Rodell, Christopher B. "An affinity for pure drugs." Science Translational Medicine 12, no. 557 (August 19, 2020): eabd4936. http://dx.doi.org/10.1126/scitranslmed.abd4936.

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26

Kwon, Soon, Ji Yu, Jihoon Kim, Hana Oh, Chan Park, Jinhee Lee, and Baik Seong. "Quality Screening of Incorrectly Folded Soluble Aggregates from Functional Recombinant Proteins." International Journal of Molecular Sciences 20, no. 4 (February 19, 2019): 907. http://dx.doi.org/10.3390/ijms20040907.

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Solubility is the prime criterion for determining the quality of recombinant proteins, yet it often fails to represent functional activity due to the involvement of non-functional, misfolded, soluble aggregates, which compromise the quality of recombinant proteins. However, guidelines for the quality assessment of soluble proteins have neither been proposed nor rigorously validated experimentally. Using the aggregation-prone enhanced green-fluorescent protein (EGFP) folding reporter system, we evaluated the folding status of recombinant proteins by employing the commonly used sonication and mild lysis of recombinant host cells. We showed that the differential screening of solubility and folding competence is crucial for improving the quality of recombinant proteins without sacrificing their yield. These results highlight the importance of screening out incorrectly folded soluble aggregates at the initial purification step to ensure the functional quality of recombinant proteins.

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27

Phan, Trang Thi Phuong. "Intracellular expression and investigation of the possibility for purifying recombinant protein in Bacillus subtilis using reporter GFP." Science and Technology Development Journal 18, no. 1 (March 31, 2015): 52–62. http://dx.doi.org/10.32508/stdj.v18i1.1034.

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most popular model organisms for Gramnegative and Gram-positive bacteria. Though this Gram-positive bacterium has a great advantage – endotoxin-free, the use of B. subtilis for expression and purification is not much interested as compared to E. coli. The reason for this is the lack of information and technology platforms on the production of recombinant proteins in B. subtilis. In the previous studies, pHT vector system has been demonstrated to allow the high levels of recombinant protein expression in B. subtilis. In this study, we used GFP as a marker for intracellular expression in B. subtilis and examining the purification capability of the recombinant protein. The expression vector was designed with gfp gen fused to the gen encoding the N-terminus of LysS protein (lysSN), His-tag and specific cleavage site of TEV protease to enhance the expression of the target protein as well as contribute to the purification and removing fusion tag afterwards. The results showed that this vector allowed the effective expression of the fusion protein LysSN- 6xHis-TEV-GFP in B. subtilis, the target protein could be purified through Ni2+ column with a high purity and fusion tag could be completely removed by TEV protease. Recombinant GFP obtained after purification was determined the molecular weight by LCMS that exhibited the analogy with the natural GFP protein. This study showed a great potential of using pHT expression system with endotoxin-free B. subtilis as a host for intracellular expression and purification of recombinant proteins.

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Huong, Phung Thi Thu, and Tran Hong Diem. "Purification of Saccharomyces cerevisiae recombinant Crp1." Journal of Science and Technology 1, no. 4 (December 25, 2018): 22–26. http://dx.doi.org/10.55401/jst.v1i4.189.

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A complex Mus81-Mm4 is a DNA structure–specific endonuclease in Saccharomyces cerevisiae. Mus81-Mms4 functions in processing of recombination intermediates that could arise during the repair of stalled and blocked replication forks and double stranded breaks. Mus81-Mms4 works with many proteins involved in DNA repair, replication fork stability, and joint molecule formation/resolution during homologous recombination repair. A biochemical screening of protein(s) that enhances the Mus81-Mms4 endonuclease activity on its preferable substrates in vitro revealed that Crp1, a cruciform DNA-recognizing protein, which can specifically bind to DNA four-way junction structures like Holliday junctions could be the potential factor. To further demonstrate that Crp1 interacts functionally with Mus81-Mms4 in vitro, we carried out the purification of recombinant Crp1 using Escherichia coli system. Our results showed that the purified Crp1 was highly homogenous and active that is ready for biochemical use.

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29

Bobek, L. A., H. Tsai, and M. J. Levine. "Expression of Human Salivary Histatin and Cystatin/ Histatin Chimeric cDNAs in Escherichia coli." Critical Reviews in Oral Biology & Medicine 4, no. 3 (April 1993): 581–90. http://dx.doi.org/10.1177/10454411930040034501.

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We have previously constructed recombinants encoding the full-length and truncated forms of cystatin-SN and expressed these in the Escherichia coli expression system pGEX-2T, which expresses foreign sequences as fusion proteins with glutathione S-transferase (GST). Recombinant cystatins were produced and purified in large quantities. The full-length recombinant cystatin-SN exhibited comparable biological activity and secondary structure to natural cystatin, validating the use of the full-length and mutant recombinant proteins for structure-function studies of salivary molecules. In this study, we have expressed histatin-1 cDNA in the pGEX-3X vector and cystatin-SN/histatin-1 or cystatin-SN/histatin-3 chimeric cDNAs in the pGEX-2T vector. Gene splicing by overlap extension (SOE), a PCR-based method, was used for generating the chimeric cDNAs. Each construct was analyzed by DNA sequencing, which showed the correct junctions and reading frames between the GST/histatin-1 and the GST/cystatin/histatin cDNAs. Expression of histatin and cystatin/histatin chimeras was induced by IPTG and the production of the fusion proteins monitored by SDS-PAGE/Coomassie blue staining and in the case of the GST/cystatin/histatin fusion proteins, also by Western blot using anti-cystatin antibody. The results of these studies showed that we have successfully constructed recombinants encoding the individual and chimeric salivary molecules and efficiently expressed these in E. coli expression system pGEX. Purification and characterization of recombinant histatin and cystatin-histatin hybrid proteins are presently ongoing.

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30

Barnard, Gavin C., Jesse D. McCool, David W. Wood, and Tillman U. Gerngross. "Integrated Recombinant Protein Expression and Purification Platform Based on Ralstonia eutropha." Applied and Environmental Microbiology 71, no. 10 (October 2005): 5735–42. http://dx.doi.org/10.1128/aem.71.10.5735-5742.2005.

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ABSTRACT Protein purification of recombinant proteins constitutes a significant cost of biomanufacturing and various efforts have been directed at developing more efficient purification methods. We describe a protein purification scheme wherein Ralstonia eutropha is used to produce its own “affinity matrix,” thereby eliminating the need for external chromatographic purification steps. This approach is based on the specific interaction of phasin proteins with granules of the intracellular polymer polyhydroxybutyrate (PHB). By creating in-frame fusions of phasins and green fluorescent protein (GFP) as a model protein, we demonstrated that GFP can be efficiently sequestered to the surface of PHB granules. In a second step, we generated a phasin-intein-GFP fusion, wherein the self-cleaving intein can be activated by the addition of thiols. This construct allowed for the controlled binding and release of essentially pure GFP in a single separation step. Finally, pure, active β-galactosidase was obtained in a single step using the above described method.

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31

Kollárovič, G., D. Majera, K. Luciaková, and P. Baráth. "Expression and purification of recombinant NFI proteins for functional analysis." General Physiology and Biophysics 28, no. 4 (2009): 331–39. http://dx.doi.org/10.4149/gpb_2009_04_331.

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32

McCluskey, Andrew J., Gregory M. K. Poon, and Jean Gariépy. "A rapid and universal tandem-purification strategy for recombinant proteins." Protein Science 16, no. 12 (December 2007): 2726–32. http://dx.doi.org/10.1110/ps.072894407.

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33

SMITH, MICHELE C. "Engineering Metal Binding Sites into Recombinant Proteins for Facile Purification." Annals of the New York Academy of Sciences 646, no. 1 Recombinant D (December 1991): 315–21. http://dx.doi.org/10.1111/j.1749-6632.1991.tb18594.x.

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34

Meyer, Dan E., and Ashutosh Chilkoti. "Purification of recombinant proteins by fusion with thermally-responsive polypeptides." Nature Biotechnology 17, no. 11 (November 1999): 1112–15. http://dx.doi.org/10.1038/15100.

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35

Kusnadi, A. R., E. E. Hood, D. R. Witcher, J. A. Howard, and Z. L. Nikolov. "Production and Purification of Two Recombinant Proteins from Transgenic Corn." Biotechnology Progress 14, no. 1 (February 6, 1998): 149–55. http://dx.doi.org/10.1021/bp970138u.

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36

Zawilak-Pawlik, Anna M., Agnieszka Kois, and Jolanta Zakrzewska-Czerwinska. "A simplified method for purification of recombinant soluble DnaA proteins." Protein Expression and Purification 48, no. 1 (July 2006): 126–33. http://dx.doi.org/10.1016/j.pep.2006.01.010.

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37

Brewer, Stephen J., and Helmut M. Sassenfeld. "The purification of recombinant proteins using C-terminal polyarginine fusions." Trends in Biotechnology 3, no. 5 (May 1985): 119–22. http://dx.doi.org/10.1016/0167-7799(85)90126-x.

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Pedersen, Jytte, Claus Emborg, Jane S�rensen, and Kirsten Biedermann. "Purification of recombinant proteins by immunoaffinity chromatography with preselected antibodies." Biotechnology Techniques 7, no. 12 (December 1993): 847–52. http://dx.doi.org/10.1007/bf00156360.

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39

Du Bois, Garrett C., Sherry P. Song, Irina Kulikovskaya, Jay L. Rothstein, Markus W. Germann, and Carlo M. Croce. "Purification and Characterization of Recombinant Forms of Murine Tcl1 Proteins." Protein Expression and Purification 18, no. 3 (April 2000): 277–85. http://dx.doi.org/10.1006/prep.1999.1186.

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La Cava, Antonio, and Salvatore Albani. "Genetic Immunization for the Recovery and Purification of Recombinant Proteins." Protein Expression and Purification 18, no. 3 (April 2000): 361–65. http://dx.doi.org/10.1006/prep.2000.1210.

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Ford, Clark F., Ilari Suominen, and Charles E. Glatz. "Fusion tails for the recovery and purification of recombinant proteins." Protein Expression and Purification 2, no. 2-3 (April 1991): 95–107. http://dx.doi.org/10.1016/1046-5928(91)90057-p.

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Pina, Ana Sofia, Christopher R. Lowe, and Ana Cecília A. Roque. "Challenges and opportunities in the purification of recombinant tagged proteins." Biotechnology Advances 32, no. 2 (March 2014): 366–81. http://dx.doi.org/10.1016/j.biotechadv.2013.12.001.

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43

Kontsekova, Eva, Antonino Cattaneo, and Michal Novak. "Quick purification of recombinant human truncated tau proteins for immunoanalysis." Journal of Immunological Methods 185, no. 2 (January 1995): 245–48. http://dx.doi.org/10.1016/0022-1759(95)00120-y.

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44

Murphy, Cheryl Isaac, Helen Piwnica-Worms, Stefan Grünwald, William G. Romanow, Nicole Francis, Hua-Ying Fan, and Sharon Marr. "Expression and Purification of Recombinant Proteins Using the Baculovirus System." Current Protocols in Molecular Biology 123, no. 1 (June 28, 2018): e61. http://dx.doi.org/10.1002/cpmb.61.

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45

Porte, Mathieu, and Shaorong Chong. "Single-process expression and purification of multiple recombinant proteins through cocultivation and affinity purification." Analytical Biochemistry 381, no. 1 (October 2008): 175–77. http://dx.doi.org/10.1016/j.ab.2008.06.018.

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46

Radhakrishnan, Anjana, Christopher M. Furze, Mohd Syed Ahangar, and Elizabeth Fullam. "A GFP-strategy for efficient recombinant protein overexpression and purification in Mycobacterium smegmatis." RSC Advances 8, no. 58 (2018): 33087–95. http://dx.doi.org/10.1039/c8ra06237d.

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47

Swennen, D., F. Rentier-Delrue, B. Auperin, P. Prunet, G. Flik, S. E. Wendelaar Bonga, M. Lion, and J. A. Martial. "Production and purification of biologically active recombinant tilapia (Oreochromis niloticus) prolactins." Journal of Endocrinology 131, no. 2 (November 1991): 219—NP. http://dx.doi.org/10.1677/joe.0.1310219.

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ABSTRACT Recombinant expression vectors carrying tilapia prolactin-I or -II (tiPRL-I or tiPRL-II) cDNA were constructed and the tiPRL-I and II proteins were produced in E. coli as inclusion bodies. These inclusion bodies were dissolved in 6 mol urea/1. Refolding of the proteins was followed by SDS-PAGE under non-reducing conditions so as to visualize the oxidized state of the molecules. Proteins tiPRL-I and tiPRL-II were purified by gel filtration and ion-exchange chromatography. The N-terminal sequence and bioactivities of both purified proteins were then analysed. Recombinant tiPRL-I and tiPRL-II induced a significant rise in plasma calcium levels as well as in mucocyte density in the abdominal skin epithelium. When tested on kidney membrane, both proteins exhibited potency in competing with 125I-labelled tiPRL-I for binding sites, but tiPRL-I seemed to be more potent than tiPRL-II in competing for these sites. The results obtained for the biological activities tested suggest that both recombinant prolactins were correctly refolded and had retained the full biological activity previously observed with the natural hormone preparations extracted from the animals. Journal of Endocrinology (1991) 131, 219–227

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48

Ecker, Jeffrey W., Greg A. Kirchenbaum, Spencer R. Pierce, Amanda L. Skarlupka, Rodrigo B. Abreu, R. Ethan Cooper, Dawn Taylor-Mulneix, Ted M. Ross, and Giuseppe A. Sautto. "High-Yield Expression and Purification of Recombinant Influenza Virus Proteins from Stably-Transfected Mammalian Cell Lines." Vaccines 8, no. 3 (August 21, 2020): 462. http://dx.doi.org/10.3390/vaccines8030462.

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Influenza viruses infect millions of people each year, resulting in significant morbidity and mortality in the human population. Therefore, generation of a universal influenza virus vaccine is an urgent need and would greatly benefit public health. Recombinant protein technology is an established vaccine platform and has resulted in several commercially available vaccines. Herein, we describe the approach for developing stable transfected human cell lines for the expression of recombinant influenza virus hemagglutinin (HA) and recombinant influenza virus neuraminidase (NA) proteins for the purpose of in vitro and in vivo vaccine development. HA and NA are the main surface glycoproteins on influenza virions and the major antibody targets. The benefits for using recombinant proteins for in vitro and in vivo assays include the ease of use, high level of purity and the ability to scale-up production. This work provides guidelines on how to produce and purify recombinant proteins produced in mammalian cell lines through either transient transfection or generation of stable cell lines from plasmid creation through the isolation step via Immobilized Metal Affinity Chromatography (IMAC). Collectively, the establishment of this pipeline has facilitated large-scale production of recombinant HA and NA proteins to high purity and with consistent yields, including glycosylation patterns that are very similar to proteins produced in a human host.

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Tailakova, E. T., S. О. Sadikaliyeva, G. O. Shynybekova, A. K. Abubakirova, K. T. Sultankulova, and O. V. Chervyakova. "CONSTRUCTION, EXPRESSION AND PURIFICATION OF BRUCELLA SPP. RECOMBINANT PROTEINS L7/L12 AND SODC IN E. COLI." Series of biological and medical 2, no. 338 (April 15, 2020): 20–30. http://dx.doi.org/10.32014/10.32014/2020.2519-1629.9.

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Brucellosis is still an important public health problem as long as natural reservoirs of infection exist. Currently, live attenuated vaccines based on strains S19, RB51 and Rev1 are used for the prevention of brucellosis in animals, the main disadvantage of which is virulence for humans. However, animal immunization programs should be implemented to reduce the incidence of humans. The development of safe and effective new generation vaccines using “omix” technology is a promising direction of vaccinology. A number of immunogenic Brucella proteins that elicit both a humoral and cellular immune response has been identified. The aim of these research was to optimize the expression and purification conditions of the Brucella spp. recombinant proteins L7/L12 and SodC. As a result, expressing plasmids pET/Br-L7/L12 and pET/Br-SodC were obtained. The parameters of target genes expression in E. coli were established and the method for purification of recombinant proteins was optimized. Purification of the L7/L12 protein was performed under hybrid conditions on HisPur agarose using a binding buffer containing 6 M guanidine hydrochloride, a wash buffer with 20 mM imidazole and an elution buffer with 300 mM imidazole. Protein SodC was purified under denaturing conditions with the addition of 1 % Triton X-100 and 1 % sodium deoxycholate to the lysis buffer. Inclusions were solubilized with a buffer containing 8 M urea and 5 mM imidazole. The target protein was eluted from HisPur agarose with buffer containing 8 M urea and 100 mM imidazole. The use of modified purification protocols made it possible to obtain purified recombinant proteins with a yield of 13 mg/L for the L7/L12 protein and 10 mg/L for the protein SodC, respectively. The specificity of the proteins was confirmed by a Western blot. Immunization of mice with recombinant proteins led to the production of specific antibodies, the titer of which in ELISA was 1:20480 and 1:20480, respectively.

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Rengachary, Setti S. "Bone morphogenetic proteins: basic concepts." Neurosurgical Focus 13, no. 6 (December 2002): 1–6. http://dx.doi.org/10.3171/foc.2002.13.6.3.

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The cellular and molecular events governing bone formation in the embryo, healing of a fractured bone, and induced bone fusion follow a similar pattern. Discovery, purification, and recombinant synthesis of bone morphogenetic proteins (BMPs) constiute a major milestone in the understanding of bone physiology. In this review the author discusses the mechanism of action, clinical applications, dosage, and optimum carriers for BMPs. The roles played by other growth factors are also discussed.

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Journal articles on the topic 'Recombinant proteins Purification'

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