Chromogenic proteinase substrates as possible tools in the characterization of Crotalidae and Viperidae snake venoms.
Proteinase activities have been determined photometrically in 25 different Crotalidae and Viperidae snake venoms by using five different chromogenic proteinase substrates. The activity profiles obtained by listing the identity numbers of substrates hydrolyzed by the venoms in a decreasing potency order remained quite stable within a given snake population. Submission of a venom to various physical and chemical treatments did not alter its activity profile. It is therefore concluded that this simple method of determining proteinase activities could be of help in snake venom characterization, as well as in studying the influence of metallic ions and inhibitors of snake venom proteinases.
D000818:Animals; D002021:Buffers; D002863:Chromogenic Compounds; D003435:Crotalid Venoms / Q000032:analysis*; D010447:Peptide Hydrolases / Q000032:analysis*; D014757:Viper Venoms / Q000032:analysis*
D002021:Buffers; D002863:Chromogenic Compounds; D003435:Crotalid Venoms; D014757:Viper Venoms; D010447:Peptide Hydrolases