par Graff, Guy ;Yager, Michèle ;Kleiner, Henri
Référence Comparative biochemistry and physiology. B, Comparative biochemistry, 49, 3, page (381-386)
Publication Publié, 1974-11
Article révisé par les pairs
Résumé : 1. 1. The presence of a l-leucyl-β-naphthylamidase activity has been demonstrated in hepatopancreas, mantle, gills, foot, siphuncles and adductor muscles of the sea mussel Mytilus edulis. 2. 2. The hepatopancreas extracts had a maximal activity against l-phenylalanyl-β-naphthylamide and were less active against l-leucyl-, l-tyrosyl- and l-tryptophanyl-β-naphthylamides, in that order. 3. 3. The l-phenylalanyl- and l-leucyl-β-naphthylamidases were maximally active at pH 7·2 with Km of respectively 2·2 × 10-4 M and 3·5 × 10-4 M and activation energies of respectively 12·3 × 103 cal and 10·7 × 103 cal. 4. 4. Both activities were inhibited by 8 M urea, p-chloromercuribenzoate, iodoacetamide and mercaptoethanol. 5. 5. The l-phenylalanyl- and l-leucyl-β-naphthylamidase activities are presumably due to a single enzyme. © 1974.