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- W2036228369 abstract "An arginine esterase was purified from the venom of Lachesis muta noctivaga by gel filtration on Sephadex G-100 and by affinity and DEAE cellulose chromatography. The purified enzyme preparation had an arginyl esterase specific activity of 181 mumoles/min/mg, which was 10.9-fold higher than the esterase activity found in the crude venom. The enzyme is free of kinin-releasing activity (kininogenase) and thrombin-like activity (fibrinogenase). The purified fraction showed a single band on polyacrylamide gel electrophoresis. The Km for Bz-L-Arg-O-Et is 1.14 X 10(-3)M, Vm 181.7 mumoles/min/mg and Kcat 90.9 sec-1. The pH profile indicates that the enzyme has an active region centered at pH 8.1. L. muta noctivaga arginyl esterase is reversibly inhibited by benzamidine (Ki 8.9 X 10(-4)M) and irreversibly inhibited by diisopropyl fluorophosphate." @default.
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- W2036228369 date "1985-01-01" @default.
- W2036228369 modified "2023-09-24" @default.
- W2036228369 title "Purification and partial characterization of an arginine ester hydrolase from the venom of the bushmaster snake, Lachesis muta noctivaga" @default.
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- W2036228369 doi "https://doi.org/10.1016/0041-0101(85)90375-7" @default.
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