Abstract
A recombinant version of the receptor binding domain (RBDv) of human α 2-macroglobulin (α 2M) has been expressed in E. coli and 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 1444 and 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 K d of 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.
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