Snake Venom Proteinases as Tools in Hemostasis Studies: Structure-Function Relationship of a Plasminogen Activator Purified from Trimeresurus stejnegeri Venom | Zendy

A. Wisner | Zendy; S. Braud | Zendy; Cassian Bon | Zendy

Open Access

Snake Venom Proteinases as Tools in Hemostasis Studies: Structure-Function Relationship of a Plasminogen Activator Purified from Trimeresurus stejnegeri Venom

Author(s) -

A. Wisner,

S. Braud,

Cassian Bon

Publication year - 2001

Publication title -

pathophysiology of haemostasis and thrombosis

Language(s) - English

Resource type - Journals

eISSN - 1424-8840

pISSN - 1424-8832

DOI - 10.1159/000048056

Subject(s) - venom , snake venom , serine , coagulation , plasminogen activator , hemostasis , biology , activator (genetics) , biochemistry , enzyme , medicine , receptor , endocrinology

Snake venom serine proteinases affect many steps of the blood coagulation cascade. Each of them usually acts selectively on one coagulation factor. They are therefore potentially useful components to study the mechanisms of action, the regulation and the structure-function relationships of human serine proteinase coagulation factors. This strategy is illustrated for a plasminogen activator purified from Trimeresurus stejnegeri venom.

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