A new fibrinogenase(EC 3.4.2 I.5)was isolated and purified from the venom of Chinese habu snake(Trimeresurus研ucrosg“ama似s)by DEAE—SephadexA-50,DEAE—Sepharose CL一6B,MonoQ(FPLC)CG.1umn chromatography.It showed a single protein band both in sodium dodeeyl sulfate(SDS)·polyacrylami-de geI electrophoresis and alkaline polyacrylamide gel electrophoresis.The molecular weight was estimated tobe 26000 by SDS·p01yacrylam|de gel electrophoresis.The isoeleetric point was found to be pH 4.7.Itwas a glycoprotein containing 6.4‘%carbohydrate with o.3%neutral sugar,1.2%sialic acid,4.9%he.xosamine.It was composed of about 1 78 amino acid residues and rich in glycine and aspartic acid.Thefibrinogenase of the venom of T.munro$quclmatu$TWV№was heat stable but labile to acid.Its extinctioncoefficient(1mg/m1)at 280rim was 1.558.Purified TMVFg had strong arginine esterase activity·the Kmto benzoylarginine ethylester(BAEE)was 1.4×1 0一M.The enzyme activity could be inhibited by pheny.1mefha口esulfonyfluoride(PMSF),but was not affected by ethylenediamine tetraacetlc acid(EDTA).TMVFghad fibrinogenolytie activityl electrophoresis of fibrinogen degraded with TMVFg revealed the rapiddisappearance of the口(alpba)and B(beta)‘chains and the appearance I】f lower molecular weight frag.merits.TMVFg did not cause fibrinogen solution clotting,nor coagulating plasma and showed n^ither hemorr-hagic activity nor proteolytic activity toward casein.TMVFg had activati^lg fibrinolytic activity
