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Specificity of Hemorrhagic Proteinase From Crotalus Atrox (Western Diamondback Rattlesnake) Venom

Y Komori, S Hagihara, A T Tu

Biochim Biophys Acta. 1985 May 20;829(1):127-30.

PMID: 3888273

Abstract:

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.

Chemicals Related in the Paper:

Catalog Number Product Name Structure CAS Number Price
IAR4245245 Snake venom from Crotalus atrox (Western Diamondback Rattlesnake) Snake venom from Crotalus atrox (Western Diamondback Rattlesnake) Price
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