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Functional and biological insights of rCollinein-1, a recombinant serine protease from Crotalus durissus collilineatus.

Johara Boldrini-França | Ernesto Lopes Pinheiro-Junior | Eliane Candiani Arantes
The journal of venomous animals and toxins including tropical diseases | 2019

The prevalent class of snake venom serine proteases (SVSP) in Viperidae venoms is the thrombin-like enzymes, which, similarly to human thrombin, convert fibrinogen into insoluble fibrin monomers. However, thrombin-like serine proteases differ from thrombin by being unable to activate factor XIII, thus leading to the formation of loose clots and fibrinogen consumption. We report the functional and biological characterization of a recombinant thrombin-like serine protease from Crotalus durissus collilineatus, named rCollinein-1.

Pubmed ID: 31131001

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GraphPad Prism (tool)

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QIAGEN (tool)

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Swiss nude (tool)

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laboratory mouse with name Swiss nude from MGI.

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