抄録
Fluorometric determination of proteinase activity was investigated by using some kinds of DNS peptides as substrates.
Fluorescence intensity of a cleft DNS peptide was measured by a fluorometer after separation from the substrate by column or thin layer chromatography, and the proteinase activity was determined in terms of moles of the hydrolyzed substrate per minute.
The method was about 100-1, 000 times more sensitive than the usual method and also selective for enzyme when a suitable substrate was used. For example, DNS-Gly-Arg-Gly-Asp, DNS-Gly-Phe NH2, Leu-ε-DNS-Lys, DNS-Gly-Phe and DNS-Gly-Arg were the specific substrates for trypsin, chymotrypsin, leucine aminopeptidase, carboxypeptidase A, carboxypeptidase B, respectively.
Moreover, kinin destroying activity in body fluids were determined by using DNS bradykinin, as a substrate.
