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- W1967467957 abstract "125-I-labelled human pregnancy zone protein complexed with chymotrypsin was removed from the circulation with a half-time of 2.3 min after intravenous injection in rats. After 6 min about 67% of the label was present in the liver and about 3% was in the spleen, both in male and in female pregnant rats. The half-time of removal was more than 30 min for native pregnancy zone protein. Uptake into other organs, including placentae and feti, was negligible. 30 pM labelled pregnancy zone protein · chymotrypsin was specifically bound to rat hepatocytes and adipocytes and to human fibroblasts and monocyte-derived macrophages at 4°C. Binding was almost completely abolished by a saturating concentrating of unlabelled α2-macroglobulin · trypsin. Binding of 15 pM labelled macroglobulin complex was completely abolished by a saturating concentration of pregnancy zone protein · chymotrypsin. In rat hepatocytes, binding of pregnancy zone protein complex was lower than that of α2-macroglobulin complex at low ligand concentrations. Half-maximal receptor occupancy was obtained with about 300 pM pregnancy zone protein complex. Unlabelled α2-macroglobulin or pregnancy zone protein complex failed to accelerate dissociation of the labelled pregnancy zone protein complex under conditions where dissociation of α2-macroglobulin was markedly enhanced. It is concluded that pregnancy zone protein and α2-macroglobulin complexes bind to the same receptors. The quantitative differences may be related to the fact that α2-macroglobulin is a tetramer whereas the functional unit of pregnancy zone protein is probably a dimer." @default.
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- W1967467957 date "1986-10-01" @default.
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- W1967467957 title "Evidence for binding of human pregnancy zone protein-proteinase complex to α2-macroglobulin receptors" @default.
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- W1967467957 doi "https://doi.org/10.1016/0304-4165(86)90276-x" @default.
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