On a plasminogen activator from human plasma.
A plasminogen activating substance was purified from the dialysates of the eluates of glass adsorbed kallikrein from fresh human plasma, by chromatography on QAE-Sephadex A-50 and gel filtration in Sephadex G-25. The preparation was concentrated by lyophilization. Its electrophoretic mobility was found to be similar to that of prealbumin. Its molecular weight appeared to be 15000-18000 daltons. The analysis of aminoacids of this activator showed that it contains a high proportion of acid amino acids. The purified activator showed esterase activity, fibrinolytic activity and kininogenase activity on heated human plasma. These activities were respectively equivalent to 150 muM BAEe/mg protein, 19 x 10(3) units of streptokinase/microgram protein and 250 microgram bradykinin/mg protein.
D000596:Amino Acids; D001798:Blood Proteins; D002850:Chromatography, Gel; D004588:Electrophoresis, Cellulose Acetate; D004591:Electrophoresis, Polyacrylamide Gel; D004950:Esterases; D005342:Fibrinolysis; D006801:Humans; D007610:Kallikreins; D008970:Molecular Weight; D010960:Plasminogen Activators / Q000097:blood* / Q000302:isolation & purification
D000596:Amino Acids; D001798:Blood Proteins; D004950:Esterases; D007610:Kallikreins; D010960:Plasminogen Activators