A comparative study of the biological properties of venoms from snakes of the genus Vipera (true adders)
1. The hemorrhagic, procoagulant, anticoagulant, phosphodiesterase, hyaluronidase, alkaline phosphomonoesterase, 5'-nucleotidase, arginine ester hydrolase, phospholipase A, L-amino acid oxidase and protease activities of 26 samples of venoms of 13 taxa of Vipera were determined and the Sephadex G-75 gel filtration patterns for some of the venoms were also examined. 2. The results indicate the presence of certain common characteristics among the venoms, particularly if V. russelli is excluded from the comparison. The results also support the recently proposed reassignment of V. russelli to a separate genus. 3. The data show that information on venom biological properties can be used for differentiation of venoms of many species of Vipera. Particularly useful for this purpose are the protease, phosphodiesterase, phospholipase A and the procoagulant activities and the Sephadex G-75 gel filtration patterns of the venoms.
Tan
N H
NH
Department of Biochemistry, University of Malaya, Malaysia.
Ponnudurai
G
G
D000818:Animals; D001777:Blood Coagulation / Q000187:drug effects; D002850:Chromatography, Gel; D010450:Endopeptidases / Q000378:metabolism; D006470:Hemorrhage / Q000139:chemically induced; D051379:Mice; D010741:Phospholipases A / Q000378:metabolism; D010727:Phosphoric Diester Hydrolases / Q000378:metabolism; D012911:Snakes / Q000378:metabolism; D013045:Species Specificity; D014757:Viper Venoms / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology
D014757:Viper Venoms; D010741:Phospholipases A; D010727:Phosphoric Diester Hydrolases; D010450:Endopeptidases