Evaluation of haemostatic activity of a serine protease isolated from S. tuberosum leaves

PEPE, A; PEDRAZA, AB; FERNÁNDEZ, MB; GALBÁN, GJ; GUEVARA, MG

Congreso; SAIB; 2014

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 μg/ml like others plant serine proteases reported. The results indicate that StSBTc-3 may have potential and therapeutic applications.