Abstract
1. 1. A new, unstable, particle-bound (particularly mitochondria and microsomes) aminopeptidase, mol. wt 74,000, was partially purified from rat liver. 2. 2. Among five aminoacyl-β-naphthylamides assayed, MetNA was the best substrate. The aminopeptidase releases NH 2-terminal methionine from methionyllysylbradykinin. 3. 3. Titration with p-hydroxymercuribenzoate indicated that this methionine aminopeptidase contains ca five SH groups per mol.
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