leupeptins has been researched along with quintozene* in 1 studies
1 other study(ies) available for leupeptins and quintozene
| Article | Year |
|---|---|
The bovine lens neutral proteinase comprises a family of cysteine-dependent proteolytic activities.
Inhibitor studies with peptide substrates demonstrate that bovine lens neutral proteinase comprises three distinct activities. Diisopropylfluorophosphate distinguishes the activity hydrolyzing carbobenzoxy-Gly-Gly-Leu-p-nitroanilide (inhibited) from that hydrolyzing carbobenzoxy-Leu-Leu-Glu-2-naphthylamide (not inhibited). Leupeptin inhibits hydrolysis of the substrate carbobenzoxy-Leu-Leu-Arg-2-naphthylamide, but not hydrolysis of carbobenzoxy-Gly-Gly-Leu-p-nitroanilide or carbobenzoxy-Leu-Leu-Glu-2-naphthylamide, demonstrating the presence of the third activity. Inhibition of the three activities by thiol reagents suggests that each activity may be dependent on an active-site cysteine residue. Topics: Animals; Cattle; Cysteine; Endopeptidases; Hydrolysis; Lens, Crystalline; Leupeptins; Neprilysin; Nitrobenzenes; Oligopeptides; Peptide Hydrolases; Protease Inhibitors; Substrate Specificity; Trypsin | 1986 |