Abstract
1. Sonication, deoxycholate treatment, freezing and thawing and mechanical grinding techniques were tried to solubilize the glutamic-pyruvic transaminase (GPT) from mitochondria and the enzymes having the same activities were obtained.
2. Glutamic-pyruvic transaminases in soluble fraction and mitochondria (GPTS and GPTM) were eluted with 0.02M phosphate buffer, pH 6.8, and 0.06M phosphate buffer, pH 6.8, respectively, in calcium phosphate gel column chromatography by stepwise and gradient eluting systems. In zone electrophoresis, they moved to the cathode and could not be separated from each other. These enzymes also have quite different optimal pH values.
3. Michaelis constants of GPT and their elementary reactions were determined and found to be almost equal in both crude and purified GPTS and GPTM reactions.
