PRODUCTION OF RECOMBINANT SERPINS IN ESCHERICHIA COLI

被引：3

作者：

Pearce, Mary C. ^{[1
]}

Cabrita, Lisa D. ^{[2
]}

机构：

[1] Monash Univ, Dept Biochem, Clayton, Vic 3168, Australia

[2] UCL, Dept Biol Mol & Struct, London, England

来源：

METHODS IN ENZYMOLOGY, VOL 501: SERPIN STRUCTURE AND EVOLUTION | 2011年 / 501卷

关键词：

PLASMINOGEN-ACTIVATOR INHIBITOR-1; EPITHELIUM-DERIVED FACTOR; CELL CARCINOMA ANTIGEN; CONFORMATIONAL-CHANGE; BIOLOGICAL-ACTIVITY; CRYSTAL-STRUCTURE; INCLUSION-BODIES; PURIFICATION; EXPRESSION; ENVIRONMENT;

D O I：

10.1016/B978-0-12-385950-1.00002-X

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Serpins represent a diverse family of proteins that are found in a wide range of organisms and cellular locations. In order to study them, most need to be produced recombinantly, as isolation from their source is not always possible. Due to their relatively uncomplicated structure (single domain, few posttranslational modifications), the serpins are usually amenable to expression in Escherichia coli, which offers a fast and cost-effective solution for the generation of large amounts of protein. This chapter outlines the general procedures used in the expression and subsequent purification of serpins in E. coli, with a particular focus on the methods used for antitrypsin, the archetypal member of the family.

引用

页码：13 / 28

页数：16

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