摘要: Summary α - L -Glutamyl peptidase activity of rat-kidney microsomes and rat serum (plasma) was studied, using as chromogenic substrates both p -nitroanilide β -naphthylamide. The latter hydrolysed at higher rates than the -nitroanilide. rate constants, pH optima, influence chelating agents suggested a close relationship this Ca 2+ -activated arylamidase to angiotensinase A. By Val 5 -angiotensin II number its derivatives competitive inhibitors, it found that -glutamyl arylamide hydrolysis inhibited greatest extent by -Asp 1 (free acid). Hydrolysis -leucyl mainly angiotensin amide. Inhibition those with were obtained hexapeptide Val-Tyr-Val-His-Pro-Phe. A group specificity for angiotensinase-like can be substrate, separated from leucyl hydrolysis.
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