Snake venom proteinases as tools in hemostasis studies: structure-function relationship of a plasminogen activator purified from Trimeresurus stejnegeri venom.
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.
Wisner
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Venoms Unit, Institut Pasteur, 27-28 rue du Docteur-Roux, F-75724 Paris Cedex 15, France.
Braud
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Bon
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C
D000818:Animals; D003435:Crotalid Venoms / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology; D006487:Hemostasis / Q000187:drug effects*; D006801:Humans; D008958:Models, Molecular; D010960:Plasminogen Activators / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology; D012697:Serine Endopeptidases / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology*; D012910:Snake Venoms / Q000201:enzymology* / Q000494:pharmacology; D013329:Structure-Activity Relationship
D003435:Crotalid Venoms; D012910:Snake Venoms; C029748:Trimeresurus venoms; D010960:Plasminogen Activators; D012697:Serine Endopeptidases