Differential inhibition of two proteolytic activities in bovine lens neutral-proteinase preparations.
Hydrolysis of carbobenzoxy-Leu-Leu-Glu 2-naphthylamide by bovine lens neutral-proteinase preparations is not affected by the esterase inhibitor di-isopropyl fluorophosphate, whereas hydrolysis of carbobenzoxy-Gly-Gly-Leu p-nitroanilide is completely inhibited. Hydrolysis of alpha-crystallin, a lens structural protein, can be inhibited by only 50% after prolonged treatment with di-isopropyl fluorophosphate. These data suggest that the lens neutral-proteinase preparation contains at least two enzymes, one of which may be a serine proteinase. This may account, in part, for the previously observed complex response of the preparation to inhibitors.
D000818:Animals; D002417:Cattle; D007527:Isoenzymes / Q000037:antagonists & inhibitors*; D007531:Isoflurophate / Q000494:pharmacology; D007908:Lens, Crystalline / Q000201:enzymology*; D008666:Metalloendopeptidases; D011480:Protease Inhibitors; D013379:Substrate Specificity
D007527:Isoenzymes; D011480:Protease Inhibitors; D007531:Isoflurophate; D008666:Metalloendopeptidases