Plasmin regulating system from embryonal carcinoma F9 cells: plasminases A, B and embrinogen.
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.
D000818:Animals; D002460:Cell Line; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D005341:Fibrinolysin / Q000378:metabolism*; D007700:Kinetics; D051379:Mice; D008970:Molecular Weight; D009363:Neoplasm Proteins / Q000302:isolation & purification* / Q000378:metabolism; D010958:Plasminogen / Q000378:metabolism; D012697:Serine Endopeptidases; D013724:Teratoma / Q000201:enzymology*
D009363:Neoplasm Proteins; D010958:Plasminogen; C040905:embrinogen; D010450:Endopeptidases; D012697:Serine Endopeptidases; C040903:plasminase A; C040904:plasminase B; D005341:Fibrinolysin