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2. Throughout purification the ratio of i8ocitricdehydrogenase activity to oxalosuccinic-carboxylase activity remains constant, and inactivation of the one produces a corresponding inactivation ofthe other. 3. Sedimentation and diffusion measurements, and electrophoretic analysis at pH 5-6, 7-3 and 8-5, show that the enzyme is a single protein. It has been obtained 90-95% pure. 4. Further fractionation of the purified enzyme confirms that it is the component representing 9095 % of the total protein which possesses both i8ocitric-dehydrogenase and oxalosuccinic-carboxylase activity. 5. The molecular weight ofthe iaocitric enzyme is approximately 64000.

Some properties of purified isocitric enzyme