Some characteristics of urokinase released in organ culture of human kidney.

Plasminogen activator produced in organ culture of human kidney, i.e. in the histotypical arrangement of the tissue, was partially purified by affinity chromatography on para-aminobenzamidine coupled to Sepharose by a 6-carbon spacer, followed by gel chromatography on Sephadex G-100. The molecular weight of 2 active peaks were 27,000 and 52,000 daltons respectively. It was inhibited by DFP and by IgG antiurokinase.