| Autor: |
Holtet, Thor Las, Nielsen, Kåre Lehmann, Etzerodt, Michael, Moestrup, Søren Kragh, Gliemann, Jørgen, Sottrup-Jensen, Lars, Thøgersen, Hans Christian |
| Zdroj: |
FEBS Letters; January 1994, Vol. 344 Issue: 2 p242-246, 5p |
| Abstrakt: |
A recombinant version of the receptor binding domain (RBDv) of human α 2-macroglobulin (α 2M) has been expressed in E. coliand refolded using a novel iterative procedure. RBDv (Val 1299-Ala 1451) is extended by 15 residues at the N-terminal side of the Lys 1313-Glu papain cleavage site in human α 2M. RBDv contains the intra-chain bridge Cys 1329-Cys 1444and is soluble and monomeric. Competition experiments with 125I-labelled methylamine-treated α 2M reveal that RBDv binds to the placental receptor for transformed α 2M with a Kdof 8 nM, i.e. the binding affinity of RBDv is of the same order of magnitude as the intrinsic affinity for binding of one domain in transformed α 2M to one receptor molecule. |
| Databáze: |
Supplemental Index |
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