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• W2035760857 abstract "The mechanisms by which alpha 1-antitrypsin and antithrombin III inhibit trypsin were investigated by chemical stability studies and amino acid sequence analyses of the enzyme-inhibitor complexes. One-to-one covalently linked complexes were formed between each of the inhibitors and trypsin. The complexes were stable over the course of the experiments at pH 8 or lower, and benzamidine, hydroxylamine, thiols, guanidine, or dodecyl sulfate had no apparent effect on the stability of the complexes. The complexes dissociated slowly at pH 9 or greater. Neither of the inhibitors was active after dissociation from its complex with trypsin. Sequence analysis indicated that no new amino terminus was generated when alpha 1-antitrypsin formed its complex with trypsin, but that two new amino termini were formed in approximately one-to-one ratio when the complex dissociated. This may indicate that alpha 1-antitrypsin contains two inhibitory sites for trypsin in close spatial proximity on the molecule." @default.
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• W2035760857 date "1980-04-01" @default.
• W2035760857 modified "2023-09-25" @default.
• W2035760857 title "Formation and Dissociation of the Covalent Complexes Between Trypsin and Two Homologous Inhibitors, alpha1-Antitrypsin and Antithrombin III" @default.
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• W2035760857 doi "https://doi.org/10.1111/j.1432-1033.1980.tb04531.x" @default.
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