title: Purification and partial characterization of an arginine ester hydrolase from the venom of the bushmaster snake, Lachesis muta noctivaga.
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.
mesh_terms: D000818:Animals; D002265:Carboxylic Ester Hydrolases / Q000032:analysis / Q000302:isolation & purification*; D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D003435:Crotalid Venoms / Q000032:analysis*; D007700:Kinetics; D008970:Molecular Weight
chemical_list: D003435:Crotalid Venoms; C019724:arginine esterase; D002265:Carboxylic Ester Hydrolases