Purification and characterization of tenerplasminin-1, a serine peptidase inhibitor with antiplasmin activity from the coral snake (Micrurus tener tener) venom

A plasmin inhibitor, named tenerplasminin-1 (TP1), was isolated from Micrurus tener tener (Mtt) venom. It showed a molecular mass of 6542Da, similarly to Kunitz-type serine peptidase inhibitors. The amidolytic activity of plasmin (0.5nM) on synthetic substrate S-2251 was inhibited by 91% following t...

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Veröffentlicht in:	Comparative biochemistry and physiology. Toxicology & pharmacology 2016-01, Vol.179, p.107-115
Hauptverfasser:	Vivas, Jeilyn, Ibarra, Carlos, Salazar, Ana M., Neves-Ferreira, Ana G.C., Sánchez, Elda E., Perales, Jonás, Rodríguez-Acosta, Alexis, Guerrero, Belsy
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Antifibrinolytic Agents - isolation & purification Antifibrinolytic Agents - pharmacology Elapid Venoms - isolation & purification Elapid Venoms - pharmacology Elapidae elastase fibrinogen Fibrinolysin - antagonists & inhibitors Fibrinolysin - metabolism Fibrinolytic system Hemostasis Humans mechanism of action metalloproteinases Micrurus Micrurus tener tener molecular weight nitroprusside plasmin Plasmin inhibitor plasminogen proteolysis Serine Proteinase Inhibitors - isolation & purification Serine Proteinase Inhibitors - pharmacology Snake venom snakes trypsin venoms
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