CATALYTIC ACTIVITIES OF CRUDE ENZYME FRACTIONS FROM MONTEREY SARDINE

Catalytic activities in sarcoplasmic fluid of Monterey sardine (Sardin ops sagax caerulea) were identified. Hydrolysis at pH 7.6 on hippuryl- L-phenylalanine and hippuryl-L-arginine suggested the presence of carb oxypeptidase A and B. Proteolysis on glutaryl-L-phenylalanine-p-nitroa nilide, and inhibition by CuSO4, phenylmethylsulfonyI fluoride and N-p -tosyl-L-lysil chloromethyl ketone, confirmed presence of a chymotryps in-like proteinase and other serine enzymes. No hydrolysis on alpha-N- benzoyl-D,L-arginine-p-nitroanilide occurred Leucine aminopeptidase wa s detected by hydrolysis on L-leucyl-beta-naphthylamide-HCl. Activity at pH 3 proved the presence of an acid proteinase but a slight inhibit ion by EDTA suggested the involvement of a cathepsin D-like enzyme. Ca thepsins A and B and collagenase were not detected.