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Acta Pol Pharm
September 2004
Department of Organic Chemistry, Medical University of Bialystok, I Kilifiskiego Str., 15-089 Bialystok, Poland.
Effect of three epsilon-aminocaproylaminoacids with a significant antifibrinolytic activity on amidolytic activity of tissue plasminogen activator (t-PA), urokinase and kallikrein was examined. epsilon-Aminocaproyl-S-benzyl)-L-cysteine and epsilon-aminocaproyl-L-norleucine were weak inhibitors of kallikrein. Weak activation of t-PA activity was observed at high concentration of the tested compounds.
View Article and Find Full Text PDFActa Pol Pharm
September 2001
Institute of Chemistry, University of Białystok, Poland.
Effect of three epsilon-aminocaproylaminoacids with significant antifibrinolytic activity on chymotrypsin, trypsin, cathepsin B, cathepsin C and cathepsin D activities was examined. Slight inhibition of trypsin and chymotrypsin activity was observed only at high concentrations of these compounds. All tested dipeptides did not influence activities of cathepsin B, cathepsin C and cathepsin D.
View Article and Find Full Text PDFMater Med Pol
May 1999
Institute of Chemistry, University in Białystok, Poland.
Influence of four epsilon-aminocaproylaminoacids on prothrombin activation and thrombin activity was examined. Only epsilon-aminocaproylnorleucine markedly inhibited the prothrombin activation in an extrinsic system.
View Article and Find Full Text PDFActa Pol Pharm
August 1998
Institute of Chemistry, Białystok University, Poland.
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