PMID: 6966218Apr 1, 1980Paper

Formation and dissociation of the covalent complexes between trypsin and two homologous inhibitors, alpha 1-antitrypsin and antithrombin III

European Journal of Biochemistry
W C MahoneyM A Hermodson

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.

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Citations

Jan 28, 1998·Arteriosclerosis, Thrombosis, and Vascular Biology·M IinoW Kisiel
Oct 29, 1982·Molecular and Cellular Biochemistry·I Björk, U Lindahl
Apr 28, 1983·Biochimica Et Biophysica Acta·D R BoswellR W Carrell
Jan 1, 1984·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·M MinnichH James
May 1, 1982·Experimental Eye Research·S S Tse, B J Ortwerth

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