Preliminary characteristics of the prothrombin converting enzyme from venom of Stephen's banded snake ( Hoplocephalus stephensii)

• Published in: Toxicon (Oxford) Vol. 39; no. 12; pp. 1937 - 1939
• Main Authors: Weinstein, S.A., Williams, V., White, J.
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 01.12.2001; Elsevier Science
• Subjects: Animal poisons toxicology. Antivenoms; Animals; Biological and medical sciences; Coagulants - isolation & purification; Coagulation Protein Disorders - blood; Elapid Venoms - chemistry; Elapid Venoms - enzymology; Electrophoresis, Polyacrylamide Gel; factor V; Factor X a; factor Xa; Factor Xa - isolation & purification; Female; Hoplocephalus; Hoplocephalus stephensii; Male; Medical sciences; Notechis scutatus; Procoagulant; prothrombin; Toxicology; Whole Blood Coagulation Time; Australia; Oceania; Hoplocephalus; Factor X a; Procoagulant; Blood coagulation; Serine endopeptidases; Enzyme; Toxicity; Animal origin; Coagulation Factor Xa; Ophidia; Peptidases; Vertebrata; Enzymatic activity; Venom; Prothrombin; Hydrolases; Isolation; Reptilia
• ISSN: 0041-0101; 1879-3150
• DOI: 10.1016/S0041-0101(01)00168-4

Stephen's banded snake ( Hoplocephalus stephensii) is an infrequently encountered Australian elapid species. The crude venom contains coagulant activity and the component responsible is a prothrombin activator requiring factor V for activity. SDS-PAGE of the isolated native protein revealed two bands at 23 and 36 kDa. These findings indicate that the procoagulant is similar to that found in the Australian tiger snake ( Notechis scutatus) and thus resembles factor Xa.