EXPRESSION OF A FUNCTIONAL ALPHA-MACROGLOBULIN RECEPTOR-BINDING DOMAIN IN ESCHERICHIA-COLI

被引：20

作者：

SALVESEN, G ^{[1
]}

QUAN, LT ^{[1
]}

ENGHILD, JJ ^{[1
]}

SNIPAS, S ^{[1
]}

FEY, GH ^{[1
]}

PIZZO, SV ^{[1
]}

机构：

[1] UNIV ERLANGEN NURNBERG,W-8520 ERLANGEN,GERMANY

来源：

FEBS LETTERS | 1992年 / 313卷 / 02期

关键词：

ALPHA-MACROGLOBULIN; PROTEIN EXPRESSION; LIPOPROTEIN RECEPTOR;

D O I：

10.1016/0014-5793(92)81443-P

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We have expressed receptor-binding domains of human alpha2-macroglobulin and rat alpha1-macroglobulin in Escherichia coli. Expression levels of both recombinants were quite high, but the human one was insoluble, probably forming inclusion bodies. The rat domain, which lacks the human disulfide, was produced in a soluble form and readily purified by two simple chromatographic steps. Purified recombinant rat alpha1-macroglobulin receptor-binding domain was fully functional in binding to the alpha-macroglobulin receptor on human fibroblasts. This 142 residue domain should serve as an excellent template for analyzing the structural requirements for alpha-macroglobulin receptor ligation and dissecting the varied biological functions resulting from such ligation.

引用

页码：198 / 202

页数：5

共 27 条

[1] LOW-DENSITY-LIPOPROTEIN RECEPTOR-RELATED PROTEIN ALPHA-2-MACROGLOBULIN RECEPTOR IS AN HEPATIC RECEPTOR FOR TISSUE-TYPE PLASMINOGEN-ACTIVATOR [J].