RESUMO
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.
