Specificity of hemorrhagic proteinase from Crotalus atrox (western diamondback rattlesnake) venom.
Hemorrhagic proteinase, HTb, isolated from Crotalus atrox (western diamondback rattlesnake) venom was studied for its specificity. HTb showed fibrinogenase activity, hydrolyzing the A alpha chain of fibrinogen first, followed by the cleavage of the B beta chain. HTb is different from thrombin and did not produce a fibrin clot. The degradation products of fibrinogen were found to be different, indicating that the cleavage sites in the A alpha and B beta chains are different from those of thrombin. N-Benzoyl-Phe-Val-Arg-p-nitroanilide was not hydrolyzed by HTb, although this substrate was hydrolyzed by thrombin and reptilase.
D000818:Animals; D001665:Binding Sites; D003435:Crotalid Venoms / Q000378:metabolism*; D010450:Endopeptidases / Q000378:metabolism*; D005337:Fibrin; D005340:Fibrinogen; D006868:Hydrolysis; D066298:In Vitro Techniques; D008666:Metalloendopeptidases; D009842:Oligopeptides; D013379:Substrate Specificity
D003435:Crotalid Venoms; D009842:Oligopeptides; C006164:S 2160; D005337:Fibrin; D005340:Fibrinogen; D010450:Endopeptidases; D008666:Metalloendopeptidases; C044577:atrolysin A