Purification and characterization of aminopeptidase from chicken intestine

An aminopeptidase was purified 839-fold with 15% recovery from chicken intestine by a procedure involving ion exchange, gel filtration,hydrophobic interaction and affinity chromatography. The enzyme is a heteridimer of subunits 94000 Da and,66000 Da. The substrate specificity of the enzyme was in the order ala > arg > leu-beta-naphthylamide. The enzyme was strongly inhibited by bestatin, puromycin, and 1, 10-phenanthroline. The aminopeptidase showed maximum activity at pH 6 and 40 to 50degreesC. The enzyme significantly differs from the hitherto known major classes of aminopeptidases from chicken tissues in terms of molecular weight and biochemical characteristics.