FEBS Letters | |
Expression and refolding of a high‐affinity receptor binding domain from rat α 1‐macroglobulin | |
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 | |
[2]Department of Molecular Biology, University of Århus, Gustav Wieds vej 10, DK-8000 Århus C, Denmark | |
[3]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
【 预 览 】
Files | Size | Format | View |
---|---|---|---|
RO201912020301756ZK.pdf | 324KB | download |