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Human pregnancy zone protein and alpha 2-macroglobulin. High-affinity binding of complexes to the same receptor on fibroblasts and characterization by monoclonal antibodies.
Van Leuven F, Cassiman JJ, Van den Berghe H. Van Leuven F, et al. Among authors: van den berghe h. J Biol Chem. 1986 Dec 15;261(35):16622-5. J Biol Chem. 1986. PMID: 2430968 Free article.
Experiments with alpha 2-macroglobulin (alpha 2M) and PZP, both modified by methylamine, showed this receptor to be identical to the previously characterized receptor for alpha 2M-proteinase complexes (Van Leuven, F., Cassiman, J.J., and Van den Berghe …
Experiments with alpha 2-macroglobulin (alpha 2M) and PZP, both modified by methylamine, showed this receptor to be identical to the previou …
Proteolysis of human alpha 2-macroglobulin without hydrolysis of the internal thiolesters or expression of the receptor recognition site.
Van Leuven F, Marynen P, Cassiman JJ, Van den Berghe H. Van Leuven F, et al. Among authors: van den berghe h. J Biol Chem. 1988 Jan 5;263(1):468-71. J Biol Chem. 1988. PMID: 2447076 Free article.
This proteolysis was obtained with a novel bacterial proteinase we recently used to isolate the receptor-binding domain from alpha 2M (Van Leuven, F., Marynen, P., Sottrup-Jensen, L., Cassiman, J.-J., and Van Den Berghe, H. (1986) J. ...This proteinase …
This proteolysis was obtained with a novel bacterial proteinase we recently used to isolate the receptor-binding domain from alpha 2M (Va
341 results