title: Species specific sensitivity towards the hemorrhagin of Ophiophagus hannah (Elapidae).
abstract: The filtration pattern of Ophiophagus hannah venom on Sephadex G-75 shows several peaks. The first peak, S1, includes high molecular weight proteins and contains the hemorrhagic and proteolytic activities. The proteolytic fractions overlap the hemorrhagic fractions, but are not identical with them. The crude venom and the high molecular weight peak have caseinase, benzoyl-L-arginine ethyl ester hydrolase and kallikrein-like activities, but not collagenase, gelatinase, thrombin, plasmin or urokinase-like activities. The hemorrhagin of Ophiophagus hannah shows species specific differences in its hemorrhagic effects: it causes hemorrhages in rabbits and hares (Lagomorpha), but not in rats, mice or guinea-pigs (Rodentia).
authors.forename: S
authors.initials: S
authors.lastname: Weissenberg
authors.forename: M
authors.initials: M
authors.lastname: Ovadia
authors.forename: E
authors.initials: E
authors.lastname: Kochva
mesh_terms: D000818:Animals; D002850:Chromatography, Gel; D004546:Elapid Venoms / Q000032:analysis / Q000633:toxicity*; D006168:Guinea Pigs; D006470:Hemorrhage / Q000139:chemically induced*; D051379:Mice; D010447:Peptide Hydrolases / Q000032:analysis; D010741:Phospholipases A / Q000032:analysis; D011817:Rabbits; D051381:Rats; D013045:Species Specificity; D013379:Substrate Specificity; D014757:Viper Venoms / Q000633:toxicity
chemical_list: D004546:Elapid Venoms; D014757:Viper Venoms; D010741:Phospholipases A; D010447:Peptide Hydrolases