Статті в журналах з теми "Recombinant proteins Purification"
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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 джерелаLeser, 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.
Повний текст джерелаWilken, 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.
Повний текст джерелаTripathi, 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.
Повний текст джерелаLevourch, 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.
Повний текст джерелаJerlström-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.
Повний текст джерелаHeijbel, 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.
Повний текст джерелаMello, 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.
Повний текст джерелаAirenne, 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.
Повний текст джерелаHarris, 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.
Повний текст джерелаDesai, 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.
Повний текст джерелаSaraswat, 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.
Повний текст джерелаRyu, 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.
Повний текст джерелаKit, 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.
Повний текст джерелаLeong, 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.
Повний текст джерелаRodell, 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.
Повний текст джерелаKwon, 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.
Повний текст джерелаPhan, 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.
Повний текст джерелаHuong, 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.
Повний текст джерелаBobek, 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.
Повний текст джерелаBarnard, 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.
Повний текст джерелаKollárovič, 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.
Повний текст джерелаMcCluskey, 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.
Повний текст джерелаSMITH, 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.
Повний текст джерелаMeyer, 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.
Повний текст джерелаKusnadi, 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.
Повний текст джерелаZawilak-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.
Повний текст джерелаBrewer, 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.
Повний текст джерелаPedersen, 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.
Повний текст джерелаDu 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.
Повний текст джерелаLa 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.
Повний текст джерелаFord, 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.
Повний текст джерелаPina, 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.
Повний текст джерелаKontsekova, 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.
Повний текст джерелаMurphy, 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.
Повний текст джерелаPorte, 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.
Повний текст джерелаRadhakrishnan, 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.
Повний текст джерелаSwennen, 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.
Повний текст джерелаEcker, 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.
Повний текст джерелаTailakova, 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.
Повний текст джерелаRengachary, 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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