The Journal of Experimental Medicine
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The Journal of Experimental Medicine, Vol 115, 695-706, Copyright, 1962, by The Rockefeller Institute

ARTICLE

THE ENHANCEMENT OF CHLOROFORM-INDUCED PLASMA PROTEOLYTIC ACTIVITY BY EPSILON AMINOCAPROIC ACID

Virginia H. Donaldson M.D.1 and Oscar D. Ratnoff M.D.1

1 From the Research Division of the Cleveland Clinic Foundation and the Department of Medicine, Western Reserve University School of Medicine, Cleveland

The proteolytic activity in chloroform-treated plasma euglobulins has been attributed to plasmin. Plasmin can digest both casein and fibrin. Epsilon aminocaproic acid, which inhibits the activation of plasminogen, the precursor of plasmin, by streptokinase, urokinase, and tissue activators enhanced the development of casein hydrolytic activity in a mixture of chloroform and plasma euglobulins. Fibrinolytic activity was also enhanced, but this was evident only if the epsilon aminocaproic acid was removed from the chloroform-treated euglobulins prior to assay. The reasons for the paradoxical enhancement of chloroform-induced casein hydrolysis by euglobulins containing epsilon aminocaproic acid are unclear. However, studies of optimal pH, heat stability, and the effect of ionic strength on the activation of the precursor of this proteolytic enzyme do not differentiate it from plasminogen.

Submitted on November 16, 1961


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