Abstract
The activities of arylaminopeptidases in the microsomal and soluble fractions of bovine dental pulp were examined using 25 amino acid β-naphthyl-amides as substrates. The arylaminopeptidase activities towards β-naphthylamides of alanine, leucine, norleucine, lysine, arginine, phenylalanine, norvaline and methionine were high in microsomal and soluble fractions of bovine dental pulp. Glycyl-prolyl β-naphthylamidase and methionyl β-naphthylamidase activities were predominantly localized in the microsomal fraction of dental pulp, whereas leucyl β-naphthylamidase activity was in the soluble fraction.
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