Plasmin regulating system from embryonal carcinoma F9 cells: plasminases A, B and embrinogen |
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Authors: | V Keil-Dlouha E Joukoff T Planchenault |
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Affiliation: | Unite de Chimie des Proteines, INSTITUT PASTEUR, 28, rue du Docteur Roux, 75724 PARIS CEDEX 15, France |
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Abstract: | Two plasmin inactivators, plasminase A and B, and their inhibitor embrinogen were isolated from embryonal carcinoma F9 cells by preparative two-dimensional electrophoresis. Plasminases A and B have molecular weights of 160,000 and 82,000, respectively. Both are serine proteinases which digest the light chain of plasmin in a time dependent inactivation process. The heavy chain of plasmin is not affected by this action. Plasminases A and B show similar specificity towards synthetic and natural polypeptide inhibitors. The interaction of the two enzymes leads to their inhibition. Embrinogen (m.w. 84,000) inhibits both plasminases A and B as well as urokinase and plasmin. Its activation by trypsin creates embrin, a proteinase directed against plasmin heavy chain. |
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Keywords: | SDS-PAGE sodium dodecylsulfate polyacrylamide gel electrophoresis DFP diisopropylfluorophosphate 2D- two-dimensional |
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