Action of Thromboplastinase on Human Brain Lipid Fractions.

Abstract

The action of the bacterial enzyme thromboplastinase (TPase) on thromboplastically active lipids of human brain was studied. In all cases, loss in clotting potency due to enzyme action was accompanied by a liberation of acid soluble organic P. Of the Folch cephalin sub-fractions studied, the inositol phosphatide component had the highest thromboplastinase labile P fraction. Thromboplastically inactive lipids were not enzyme labile. An unidentified P containing compound was isolated from the reaction mixture after TPase action.