Abstract
Two molar potassium thiocyanate exract of psoriatic scales demonstrated fibrinolytic activity only in the pesence of plasminogen (0.54+0.51IU/mg protein). The extract also showed high level of activity on Ile-Pro-Arg-p-nitroanilide (pNA) (3.98±1.43nmol/min/mg protein). Sephacryl S-200 gel chromatography revealed that plasminogen activator (PA) activity positioned at approximately MW 60K. This PA activity was totally adsorbed to benzamidine-Sepharose column and dissociated with 2M KSCN. Enzymographic analysis demonstrated 62K, 43K and 33K PA in the adsorbed fraction. By the following high performance anion-exchange chromatography on Mono Q, three peaks of PA activities were separated. Among them, the major peak of PA activity was 62K. Futhermore, anti-urokinase (UK) IgG-Sepharose affinity chromatography of S-200 PA fraction showed that only 62K PA is adsorbed to this column and represents 70% of the total psoriatic PA activity. In order to demonstrate the localization of UK-type PA antigen in psoriatic epidermis, we performed an immunofluorescence study. UK-type PA was mainly found in upper layer of psoriatic epidermis, although diffuse fluorescence was seen in whole psoriatic epidermis.
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