Expression and refolding of a high‐affinity receptor binding domain from rat α 1‐macroglobulin

FEBS Letters

Thøgersen, Hans C.³  Fey, Georg H.¹  Sottrup-Jensen, Lars²  Nielsen, Kåre L.³ 

[1] Department of Microbiology, Biochemistry and Genetics, Universität Erlangen, D-852 Erlangen, Germany;Department of Molecular Biology, University of Århus, Gustav Wieds vej 10, DK-8000 Århus C, Denmark;Laboratory of Gene Expression, Department of Chemistry, University of Århus, Gustav Wieds vej 10, DK-8000 Århus C, Denmark

关键词: α-Macroglobulin;    Domain structure;    Protein expression;    α 2-Macroglobulin receptor;    Refolding;    in vitro;    RBD;    receptor binding domain (approx. 138 C-terminal residues);    RBDv;    receptor binding domain variant (approx. 153 C-terminal residues);    α1M;    rat α 1-macroglobulin;    α 2M;    human α 2-macroglobulin;    α 1M-MA;    methylamine treated rat α 1− macroglobulin;    α 2M-MA;    methylamine treated human α 2-macroglobulin;    α 2MR/LRP;    a2macroglobulin receptor/low density lipoprotein receptor-related protein;    α 2M-RAP;    α 2-macroglobulin receptor associated protein;    α 1M;    LC;    α 1-macroglobulin light chain;    FXa;    activated blood coagulation factor X;    GSH;    reduced glutathione;   

DOI  :  10.1016/0014-5793(95)01064-L

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A recombinant version of the receptor binding domain of rat α ₁-macroglobulin (RBDv) consisting of residues 1319–1474 has been expressed in E. coli. Competition experiments with ¹²⁵I-labelled methylamine treated human α ₂-macroglobulin reveal that the α ₁-macroglobulin-RBDv exhibit the same high affinity or the α ₂-acroglobulin receptor as the entire 40 kDa light chain from rat α ₁-macroglobulin. It is therefore concluded, that all determinants for receptor interaction reside in the C-terminal approx. 150 residues of the α-macroglobulin subunit.

【 授权许可】

Unknown