Production enhancement and refolding of caprine growth hormone expressed in Escherichia coli

Protein Expression and Purification

Volumn 68, Issue 1, 2009, Pages 85-89

  Khan, Muhammad Altaf ^a   Sadaf, Saima ^a   Sajjad, Muhammad ^a   Waheed Akhtar, M ^a  

^a UNIVERSITY OF THE PUNJAB   (Pakistan)

Author keywords

Caprine growth hormone; Production enhancement; Refolding

Indexed keywords

GROWTH HORMONE; ISOPROPYL THIOGALACTOSIDE; LACTOSE; RECOMBINANT PROTEIN;

AFFINITY CHROMATOGRAPHY; ANIMAL; ARTICLE; CELL PROLIFERATION; CHEMISTRY; CULTURE MEDIUM; ESCHERICHIA COLI; GENETICS; GOAT; MASS SPECTROMETRY; METABOLISM; PH; PILOT STUDY; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN FOLDING; RAT; TUMOR CELL LINE;

ANIMALS; CELL LINE, TUMOR; CELL PROLIFERATION; CHROMATOGRAPHY, AFFINITY; CULTURE MEDIA; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; GOATS; GROWTH HORMONE; HYDROGEN-ION CONCENTRATION; ISOPROPYL THIOGALACTOSIDE; LACTOSE; PILOT PROJECTS; PROTEIN FOLDING; RATS; RECOMBINANT PROTEINS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

CAPRA; ESCHERICHIA COLI; RATTUS;

EID: 68349141668     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2009.05.011     Document Type: Article

References (23)

1. Studier F.W. Protein production by auto-induction in high-density shaking cultures. Protein Exp. Purif. 41 (2005) 207-234
2. Fahnert B., and Lilie Hand Neubauer P. Inclusion bodies formation and utilization. Adv. Biochem. Eng. Biotechnol. 89 (2004) 93-142
3. Singh S.M., and Panda A.K. Solubilization and refolding of bacterial inclusion body protein. J. Biosci. Bioeng. 99 (2005) 303-310
4. Vallejo L.F., and Rinas U. Strategies for the recovery of active proteins through refolding of bacterial inclusion body proteins. Microb. Cell Fact. 3 (2004) 11
5. Sadaf S., Khan M.A., Wilson D.B., and Akhtar M.W. Molecular cloning, characterization, and expression studies of water buffalo (Bubalus bubalis) somatotropin. Biochemistry (Moscow) 72 (2007) 194-202
6. Khan M.A., Sadaf S., and Akhtar M.W. Role of silent gene mutations in the expression of caprine growth hormone in Escherichia coli. Biotechnol. Prog. 23 (2007) 1049-1052
7. Sambrook J., and Russell D.W. Molecular Cloning: A Laboratory Manual (2001), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
8. Sadaf S., Khan M.A., and Akhtar M.W. Production of bubaline somatotropin by auto-induction in Escherichia coli. Biochem. Appl. Biotechnol. 47 (2007) 21-26
9. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
10. Donovan R.S., Robinson C.W., and Glick B.R. Review: Optimizing inducer and culture conditions for expression of foreign proteins under the control of the lac promoter. J. Ind. Microbiol. 16 (1996) 145-154
11. Woyski D., and Cupp-Vickery J.R. Enhanced expression of cytochrome P450s from lac-based plasmids using lactose as the inducer. Arch. Biochem. Biophys. 388 (2001) 276-280
12. Kweon D.H., Han N.S., Park K.M., and Seo J.H. Overproduction of Phytolacca insularis protein in batch and fed-batch culture of recombinant Escherichia coli. Process Biochem. 36 (2001) 537-542
13. Sunitha K., Kim Y.O., Lee J.K., and Oh T.K. Statistical optimization of seed and induction conditions to enhance phytase production by recombinant Escherichia coli. Biochem. Eng. J. 5 (2000) 51-56
14. Jeong K.J., and Lee S.Y. High level production of human leptin by fed-batch cultivation of recombinant Escherichia coli and its purification. Appl. Environ. Microbiol. 65 (1999) 3027-3032
15. Przybycien T.M., Dunn J.P., Valax P., and Georgiou G. Secondary structure characterization of ß-lactamase inclusion bodies. Protein Eng. 7 (1994) 131-136
16. Oberg K., Chrunyak B.A., Wetzel R., and Fink A.L. Native like secondary structure in interleukin-1b inclusion bodies by attenuated total reflectance FTIR. Biochemistry 33 (1994) 2628-2634
17. Khan R.H., Appa Rao K.B.C., Eshwari A.N.S., Totey S.M., and Panda A.K. Solubilization of recombinant ovine growth hormone with retention of native like secondary structure and its refolding from the inclusion bodies of E. Coli. Biotechnol. Prog. 14 (1998) 722-728
18. Singh S.M., Upadhyay A.K., and Panda A.K. Solubilization at high pH results in improved recovery of proteins from inclusion bodies of E. coli. J. Chem. Technol. Biotechnol. 83 (2008) 1126-1134
19. Nall B.T., Osterhout Jr. J.J., and Ramdas L. PH dependence of folding of iso-2-cytochrome C. Biochemistry 27 (1988) 7310-7314
20. Patra A.K., Mukhopadhyay R., Mukhija R., Krishnan A., Garg L.C., and Panda A.K. Optimization of inclusion bodies solubilization and renaturation of recombinant human growth hormone from Escherichia coli. Protein Exp. Purif. 18 (2000) 182-192
21. Holzman T.F., Dougherty J.J., Brems Jr. D.N., and MacKenzie N.E. pH induced conformational state of pituitary growth hormone. Biochemistry 29 (1990) 1255-1261
22. Sereikaite J., Statkute A., Morkunas M., Radzevicius K., Borromeo V., Secchi C., and Bumilis V.A. Production of recombinant mink growth hormone in E. coli. Appl. Microbiol. Biotechnol. 74 (2007) 316-323
23. Mukhopadhyay U.K., and Sahni G. Production of recombinant buffalo (Bubalus bubalis) and goat (Capra hircus) growth hormones from genetically modified E. coli strains. J. Biotechnol. 97 (2002) 199-212