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One of the hepatic glucose 6-phosphate dehydrogenase isozymes of rats, designated "C," has been degraded by tryptic digestion into two enzymatically active forms of different electrophoretic mobility. The modified forms exhibited the same substrate specificity and mobility as the isozymes previously designated E and E'. The results of the present study emphasized that zymograms of tissues rich in proteinases should be interpreted with caution.

DEGRADATION OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE INTO ENZYMATICALLY ACTIVE MOLECULAR FORMS BY TRYPSIN