Comparative kinetic studies of the primary specificity of bovine and salmon trypsin
Taran, L.D.; Smovdyr', I.N.
Biokhimiia 57(1): 55-60
1992
ISSN/ISBN: 0320-9725 PMID: 1391204 Document Number: 390013
A comparative kinetic analysis of Pacific salmon and bovine trypsins revealed that the former hydrolyzes p-nitroanilide-N,L-benzoyl-D,L-arginine (BApNA) with a far greater efficiency in comparison with bovine trypsin due to the decrease in Km. The inhibition constants for the BApNA hydrolysis by bovine and salmon trypsin with glycine, beta-alanine, L-lysine, L-arginine and benzamidine were determined. With an increase in the length of the hydrocarbon chain in the inhibitor molecule (i.e., in the order of glycine-beta-alanine-L-lysine) the inhibiting effect increased both with salmon and bovine trypsins. The Ki values for benzamidine and L-arginine appeared to be by one order of magnitude higher with salmon trypsin than with bovine trypsin. L-arginine was a much more effective inhibitor compared to L-lysine when both salmon and bovine trypsins were used.