A fibrinogenolytic prot¢ina~¢ has been i¢olated from Aspetgillusfumbl(ausculture filtrate by ammonium sulfate precipitation followed by s~ua~.~iive ¢hromatographies on $¢phadcx G-75 and immobilized phcnylalanine, 'l'h¢ purified protein:ts¢ exhibited a molecular wright of about 33 kDa. When analysed by SDS.polyacrylamide lels containing ¢o.polymerized fibrinogen, the proteinase apixared as a broad band at the top of the ~ls. whkh could correspond to polymerization of the enzyme, as suill;¢sted by SDS-PAGE analysis of the unboiled eta,ate, The i~l¢¢tri¢ point wa~ ~,?fi and the enzyme was not lltlycosylated. Proteinus¢ activity was optimum at pH 9 and I.~tween 37 and 42"C. although a d~reaJ¢ in a~:tivity was ob~rvgl above 3"/'C. PMSF and ehymostatin markedly inhibited the protelna~ activiW, and good kinetic constants ~¢re obtained for the synthetic sabstrate. H.Suc-Ala-Ala.Pro.Phe.pNA. The~ results provide direct evidence that this enzyme belonlp to the ehymotrypsin.lik¢ =fine proteina¢ ~oup.Enzyme' purilieation: Serine proteinase: Fibrinollenolyti¢: Aspergillusfun)igutus
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