H-D-val-leu-lys-aminoisophthalic acid, dimethyl ester, is sensitive to streptokinase-activator not to plasmin.
The ability of human plasma and purified human plasmin and plasminogen to hydrolyze a new synthetic substrate, H-D-valine-leucine-lysine-5-aminoisophthalic acid, dimethyl ester, ditrifluoroacetate, was studied. Contrary to published data, we found this substrate was only minimally hydrolyzed by plasmin or urokinase-treated plasminogen or plasma. Plasminogen-free bovine fibrinogen was readily degraded by plasmin and urokinase-activated plasminogen. However, in the presence of streptokinase, the synthetic substrate was highly sensitive to human plasma and purified plasmin and plasminogen. Apparently, the substrate is specific for streptokinase-plasmin and streptokinase-plasminogen activators, not for plasmin.
D004789:Enzyme Activation; D005341:Fibrinolysin / Q000378:metabolism*; D005456:Fluorescent Dyes; D006801:Humans; D008722:Methods; D010795:Phthalic Acids; D010960:Plasminogen Activators / Q000378:metabolism; D013300:Streptokinase / Q000378:metabolism*; D013379:Substrate Specificity; D014568:Urokinase-Type Plasminogen Activator
D005456:Fluorescent Dyes; D010795:Phthalic Acids; C028924:valine-leucine-lysine-5-aminoisophthalic acid dimethyl ester; D013300:Streptokinase; D010960:Plasminogen Activators; D005341:Fibrinolysin; D014568:Urokinase-Type Plasminogen Activator