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

[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.

[学科分类] 生物化学/生物物理

[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