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- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제20권 제1호
- 발행연도
- 2010.1
- 수록면
- 132 - 137 (6page)
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The skc gene encoding streptokinase (SK) with a molecular mass of approximately 47.4 kDa was cloned from Streptococcus equisimilis ATCC 9542 and heterologously overexpressed in Streptomyces lividans TK24 and E. coli using various strong promoters. When the promoter for sprT [Streptomyces griseus trypsin (SGT)] was used in the host S. lividans TK24, a 47.4-kDa protein was detected along with a smaller hydrolyzed protein (44 kDa), suggesting that posttranslational hydrolysis had occurred as has been reported in other expression systems. The casein/plasminogen plate assay revealed that the plasmid construct containing the SGT signal peptide was superior to that containing the SK signal peptide in terms of SK production. Maximal production of SK was calculated to be about 0.25 unit/ml of culture broth, a value that was five times higher than that obtained with other expression systems using ermE and tipA promoters in the same host. When the skc gene was expressed in E. coli BL21(ΔDE3)pLys under the control of the T7 promoter, a relatively large amount of SK was expressed in soluble form without hydrolysis. SK activity in E. coli/pET28a-T7pSKm was more than 2 units/ml of culture broth, even though about half of the expressed protein formed an inactive inclusion body.
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참고문헌 (25)
참고문헌 신청
Boyle, M. D / 1997 / Plasminogen activation by invasive human pathogens / Thromb. Haemost 77 : 1 ~ 10
Bradford, M. M / 1976 / A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding / Anal. Biochem 72
Castellino, F. J / 1976 / Streptokinase / Methods Enzymol 45 : 244 ~ 257
Cherish Babu, P. V / 2008 / Renaturation, purification and characterization of streptokinase expressed as inclusion body in recombinant E. coli / J. Chromatogr. B Analyt. Tec
Christen, E. H / 2009 / A general strategy for the production of difficult-to-express inducer-dependent bacterial repressor proteins in Escherichia coli / Protein Expr. Purif
Bradford, M. M / 1976 / A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding / Anal. Biochem 72
Castellino, F. J / 1976 / Streptokinase / Methods Enzymol 45 : 244 ~ 257
Cherish Babu, P. V / 2008 / Renaturation, purification and characterization of streptokinase expressed as inclusion body in recombinant E. coli / J. Chromatogr. B Analyt. Tec
Christen, E. H / 2009 / A general strategy for the production of difficult-to-express inducer-dependent bacterial repressor proteins in Escherichia coli / Protein Expr. Purif
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