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In the presence of 10mM triethanolamine, the fibrin-binding ability of urokinase (UK) in freshly obtained human urine was compared to that of commercially obtained urinary UK and two different sources of human malignat melanoma tissue plasminogen activator (TPA). In contrast to the non-binding property to a fibrin/Celite column of commercially obtained UK, which had molecular weights (MW) of approximately 50, 000 and 30, 000 by a zymographic method, fresh urine contained at least three different molecular forms of fibrin-binding UK, all of which were adsorbed on the fibrin/Celite column at neutral pH, and could be eluted with 0.3-1.0M NaCl in phosphate buffer, 0.2M Arg, 2M KSCN, and 2M urea, respectively. The main fibrin-binding UK was a high molecular form of MW approximately 100, 000, and the minor ones were of MW 150, 000-200, 000 and 45, 000.On the other hand, most of the TPA derived from human cell cultured melanoma (Bowes) was found to be fibrin-non-binding, although TPA extracted from human melanoma tissue with 2M KSCN showed a fibrin-binding property. In the latter, PA activity was completely adsorbed and could be eluted with 6M urea buffer.These findings strongly indicate that the fibrin-binding property of PA is related to the molecular forms of PA, and is not directly dependent on their sources.
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