EVALUATION OF HAEMOSTATIC ACTIVITY OF A SERINE PROTEASE

PEPE, A.; FERNANDEZ, MB; DALEO GR; GUEVARA, MG

Rosario

Congreso; Reunión anual de la Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; 2014

Sociedad Argentina de Investigación en Bioquímica y Biología Molecular

Blood coagulation and fibrinolysis, two important processes associated with haemostasis and wound healing, involve a series of serine proteases. Fibrinogenolytic activity and anticoagulant ability of several plant serine proteases have been reported. Previously, we have reported the purification and partial characterization of a serine protease from Solanum tuberosum leaves, named as StSBTc-3. The aim of this study was to evaluate the fibrinogenolytic and anticoagulant capacity of StSBTc-3. The fibrinogenolytic activity of StSBTc-3 was analyzed by SDS-PAGE 10%, incubating different amounts of StSBTc-3 at several times (0-6 hours) with human fibrinogen isolated from human serum plasma. Thrombin time of pooled normal human plasma was determined to evaluate anticoagulant activity of StSBTc-3. The results obtained here show that StSBTc-3 is able to degrade human fibrinogen in a dose dependent manner. Contrary to the results obtained for other plant serine proteases, StSBTc-3 is able to cleave all chains of human fibrinogen. Thrombin time results show that StSBTc- 3 has anticoagulant activity in a dose dependent manner, being the maximum effect at 14 ìg/ml like others plant serine proteases reported. The results indicate that StSBTc-3 may have potential and therapeutic applications.