RESUMEN
Objective: To investigate the method for study on the effect of factors on pepsin and trypsin fibrinolytic activity and deactivation of fibrinolytic activity and to eliminate the interference of pepsin and trypsin on the detection of crude protein fibrinolytic activity of Armadillidium vulgare (porcellio plasmin) in order to obtain the proteins or peptides which have the smaller molecular weight but higher titer during the pepsin and trypsin degradation. Methods: To study the effect of pepsin and trypsin deactivation on pH value, temperature, metal ions, enzyme inhibitor, surfactant, and responsing fibrinolytic by fiber fibrin plate assay. The better enzyme deactivation process was obtained and used for studying the effect on the fibrinolytic activity of urokinase, lumbrokinase, and porcellio plasmin. Results: All the pH value, temperature, metal ions, enzyme inhibitor, and surfactant have had an impact on pepsin and trypsin fibrinolytic activity. Among them the optimum deactivation of pepsin was pH 6.0-8.0, while the optimum deactivation of trypsin was mixed preparation with TLCK at the concentration of 25 mg/mL and EDTA at the concentration of 1 mmol/L. Conclusion: This study has obtained the better enzyme deactivation process which could be used for the detection of fibrinolytic activity of pepsin and trypsin degradation product by fiber fibrin plate assay, the operation is simple, and the repeatability and stability are good.