Abstract
Four kinds of the enzyme reactions have been reported for the synthesis of Glc-1, 6-P2. However, any activity of Glc-1-P dismutase and phosphoglucokinase was not observed in the beef liver homogenate. When the liver homogenate was incubated with Glc-1-P and Fru-1, 6-P2, a significant amount of Glc-1, 6-P2 was formed. The Glc-1, 6-P2 synthesis activity from Glc-1-P and Fru-1, 6-P2 was caused by the action of phosphoglucomutase present in the liver homogenate. The most remarkable activity for Glc-1, 6-P2 synthesis was observed when the homogenate was incubated with Glc-1-P and glycerate-1, 3-P2. The Glc-1, 6-P2 synthesis activity from Glc-1-P and glycerate-1, 3-P2 was separated from the major peak of phosphoglucomutase activity by DEAE-Sephadex chromatography. The peak of Glc-1, 6-P2 synthesis activity, however, still retained phosphoglucomutase activity.
Glc-1, 6-P2 phosphatase activity was mainly observed in the mitochondria and microsome fraction. The properties of Glc-1, 6-P2 phosphatase were differentiated from those of acid phosphatase and Glc-6-P phosphatase.
