Isolation of Three Acid Phosphatases from Wheat Germ

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Abstract
Three different forms of acid phosphatase have been isolated from commercial wheat germ by ion‐exchange chromatography on DEAE‐cellulose. The three components could not be separated by gel‐filtration, suggesting that the enzyme was homogeneous with respect to molecular weight. A molecular weight of 55000 was obtained for all the three isoenzymes, as determined by gel‐filtration on Sephadex G‐100 and Sephadex G‐200. The isoenzymic nature of the three forms was suggested by differences in their pH optima, Michaelis constants, response to activation and inhibition, substrate specificities and electrophoretic mobilities. The isolation procedure was readily adapted to the preparation of large quantities of the isoenzymes. These partially‐purified forms were electrophoretically indistinguishable from the three components which could be demonstrated in the original wheat‐germ extract.