Separation of Plasma Kallikrein and a Kallikrein-like Plasminogen Activator Generated by Acetone in Rat Plasma

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Abstract
Plasminogen activator (PGA), kininogenase (Kase) and benzoyl arginine ethyl ester (BAE) activities generated in plasminogen-free rat plasma by incubation with acetone (23% vol/vol) at 22.degree. were purified. The activities passed unadsorbed through columns of DEAE-Sephadex A-50 (pH 7.8) and arginine methylester-Sepharose 4B (pH 8.5). A part of the activities (rat plasma kallikrein) was adsorbed onto a soybean trypsin inhibitor (SBTI)-Sepharose 4B column at pH 8.5. At pH 7.0 a fraction with higher ratios PGA[prostaglandin A]/BAEe esterase and Kase/BAEe esterase was also adsorbed. Both fractions could be eluted with 5 mM NaOH. The fraction not adsorbed at pH 8.5, but adsorbed at pH 7.0 was designated low MW plasminogen activator (LM PGA), a plasminogen activator fraction with higher MW, but without esterase activity being also present. LM-PGA was strongly inhibited by tranexamic acid (AMCA) 0.10 mM, whereas the fraction designated rat plasma kallikrein was not. By polyacrylamide gel electrophoresis M values in the range 120,000-130,000 were established for native samples of both rat plasma kallikrein and LMr-PGA, whereas M values of 78,000-80,000 were established after treatment with SDS [sodium dodecyl sulfate].

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