CHARACTERIZATION OF INCLUSION-BODIES IN RECOMBINANT ESCHERICHIA-COLI PRODUCING HIGH-LEVELS OF PORCINE SOMATOTROPIN

被引：37

作者：

RINAS, U

BOONE, TC

BAILEY, JE

机构：

[1] AMGEN INC, THOUSAND OAKS, CA 91320 USA

[2] CALTECH, DIV CHEM & CHEM ENGN, PASADENA, CA 91125 USA

来源：

JOURNAL OF BIOTECHNOLOGY | 1993年 / 28卷 / 2-3期

基金：

美国国家科学基金会;

关键词：

ESCHERICHIA-COLI; INCLUSION BODIES; PORCINE SOMATOTROPIN; PROTEIN COMPOSITION;

D O I：

10.1016/0168-1656(93)90179-Q

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

The protein composition of inclusion bodies (IBs) formed in recombinant Escherichia coli producing high levels of porcine somatotropin (pST) was analyzed by one- and two-dimensional protein gel electrophoresis. Recombinant pST is exclusively recovered from the insoluble cell fraction. Results indicate that, in addition to the main species of pST, subspecies with different isoelectric points and degradative fragments are contained within IBs. The presence of outer membrane proteins in IB fractions results from coprecipitation of cell debris during IB preparation and not from specific in vivo or in vitro interaction of these proteins with IBs. Cells producing pST contain up to three IBs located in the cytoplasm. The implication of high level gene expression on the uniformity of the desired product is discussed.

引用

页码：313 / 320

页数：8

共 23 条

[1] REMOVAL OF A PROTEOLYTIC ACTIVITY ASSOCIATED WITH AGGREGATES FORMED FROM EXPRESSION OF CREATINE-KINASE IN ESCHERICHIA-COLI LEADS TO IMPROVED RECOVERY OF ACTIVE ENZYME [J].