Purification of aminopeptidase a in human serum and degradation of angiotensin II by the purified enzyme

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Abstract 1. 1. Aminopeptidase A, which is activated by Ca 2+ and specifically hydrolyzes N-terminal dicarboxylic amino acids, was purified from human serum approx. 700-fold. α- l -Glutamyl β-naphthylamide was used as substrate throughout the purification. 2. 2. The purified enzyme hydrolyzed α- l -glutamyl β-naphthylamide, α- l -aspartyl β-naphthylamide, and aspartylalanine, which indicated that this enzyme preferentially hydrolyzes N-terminal dicarboxylic amino acids. Leucyl β-naphthylamidase activity was decreased during the purification, but complete removal of leucyl β-naphthylamidase activity from glutamyl β-naphthylamidase activity was not possible. 3. 3. Purified aminopeptidase A removed the N-terminal aspartic acid residue from natural angiotensin II, i.e. α- l -Asp 1 -Val 5 -angiotensin II. Thus aminopeptidase A was proved to be an “angiotensinase”. Leucyl β-naphthylamidase hydrolyzed mainly synthetic asparaginyl angiotensin II.

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