Dextran‐Induced Lowering of Plasminogen Proactivator and Functionally Active High Molecular Weight Kininogen in the Rat

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Abstract
Incubation of plasminogen‐free rat citrated plasma with acetone (23% v/v) yielded enzyme preparations with high levels of plasminogen activator (PGA) and kininogenase (kallikrein), but with a low concentration of high molecular weight kininogen (HMWK) active as cofactor for kaolin‐induced activation of factor XII. When benzamidine (4.0 mM) was present during acetone activation, a high yield of functionally active HMWK was obtained. Gel chromatography separated PGA into one high molecular weight fraction (HMW‐PGA) without kininogenase and BAEe esterase activity, and one fraction (LMW‐PGA) eluting together with plasma kallikrein. Injection of dextran (100 mg/kg intravenously) reduced the amount of LMW‐PGA to 40%, without altering the concentration of HMW‐PGA, and with only a small reduction of the kininogenase activity.