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• W2064137749 abstract "The interaction α 2 -macroglobulin with four proteinases has been investigated by binding assays and by gel electrophoresis. At pH 7.65 the binding ratios of the proteinase- α 2 -macroglobulin complexes were found to be 2:1 (trypsin and papain), 1.4:1 (chymotrypsin), and 1:1 (plasmin). The progressive decrease in the stoichiometry of the three seryl proteinase complexes was paralleled by a concomitant decrease in the proteinase-dependent specific cleavage of the α 2 -macroglobulin peptide chains. Rate studies have shown that the relative rates of reaction of the proteinases with α 2 -macroglobulin also varied greatly: papain > trypsin > chymotrypsin > plasmin. The data suggest that the ability of a proteinase to saturate the second proteinase binding site is a reflection of its ability to bind to α 2 -macroglobulin and cleave the second pair of scissile α 2 -macroglobulin peptide bonds before the α 2 -macroglobulin has undergone the conformational change initiated by the formation of the 1:1 proteinase α 2 -macro-globulin complex." @default.
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• W2064137749 date "1983-02-01" @default.
• W2064137749 modified "2023-09-24" @default.
• W2064137749 title "Interaction of α2-macroglobulin with trypsin, chymotrypsin, plasmin, and papain" @default.
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• W2064137749 doi "https://doi.org/10.1016/0003-9861(83)90143-1" @default.
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