| Literature DB >> 3893422 |
B J Wagner, J W Margolis, A S Abramovitz, S C Fu.
Abstract
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.Entities:
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Year: 1985 PMID: 3893422 PMCID: PMC1145011 DOI: 10.1042/bj2280517
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857