Silva L M, Diniz C R, Magalhães A
Toxicon. 1985;23(4):707-18. doi: 10.1016/0041-0101(85)90375-7.
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.
