EC Number |
Natural Substrates |
---|
3.4.21.68 | more |
the kringle domains 1 and 2 of tissue-type plasminogen activator, TK12, interact with endothelial vein cells via integrin and the kringle domain DGDA amino acid sequence, overview |
3.4.21.68 | more |
both plasminogen activation and fibrin lysis by tPA. Lysis of fibrin clots performed using confocal microscopy in conjunction with tPA-GFP added to clots formed of fibrin100 and fibrin5. The front of the fibrin clot moves faster in fibrin5 than in fibrin100. There are also morphologic differences that develop in the 2 fibrins as indicated by the pattern of fluorescence, which reflects tPA distribution. Specifically, it can be seen that a granular pattern develops in the fibrin5 lysis series in contrast to the homogeneous fluorescence pattern that is maintained in the fibrin100 series. Binding analysis of tPA to aggregates formed in fibrin5, using orange fluorescent fibrinogen converted to fluorescent fibrin100 and fibrin5 |
3.4.21.68 | more |
ZIP4 physically interacts with tPA, immunohistochemic analysis, overview |
3.4.21.68 | more |
the enzyme converts plasminogen into plasmin |
3.4.21.68 | N-methyl-D-aspartate receptor NR1 subunit + H2O |
- |
3.4.21.68 | plasminogen + H2O |
- |
3.4.21.68 | plasminogen + H2O |
cleavage of the Arg561-Val562 bond of plasminogen, converting the zymogen into the active serine protease plasmin |
3.4.21.68 | plasminogen + H2O |
single-chain tPA mediated activation |
3.4.21.68 | plasminogen + H2O |
critical role in fibrinolysis |
3.4.21.68 | plasminogen + H2O |
activation |