Reaction of calcium-activated neutral protease (CANP) with an epoxysuccinyl derivative (E64c) and iodoacetic acid.

摘要: The reaction of calcium activated neutral protease (CANP) with an epoxysuccinyl derivative (E64c) and iodoacetic acid (IAA) was examined in the presence Ca2+, which specifically accelerates rate inactivation by these inhibitors. 1. E64c IAA (100-fold molar excess) each inactivated CANP within a few minutes at 0 degrees C. Upon inactivation, 1 mol or incorporated into CANP. optimal pH 7.5-8.0, where shows maximum enzyme activity. 2. modified lost one 3 SH groups (class II groups) were exposed surface addition Ca2+. No conformation change observed as result modifications. 3. Leupeptin inhibited A total successive labeling IAA. It concluded from results that react same class group, is regarded active site