Studies on the Formation and the Degradation of Glucose 1,6-Bisphosphate in the Beef Liver Homogenate |
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Authors: | Masatsugu Ueda Masaaki Hirose Hideo Chiba |
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Affiliation: | Department of Food Science and Technology, Faculty of Agriculture, Kyoto University, Kyoto 606, Japan |
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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. |
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Keywords: | aldo-keto reductase (AKR) cyanobacteria medium-chain dehydrogenase/reductase (MDR) short-chain dehydrogenase/reductase (SDR) glyoxalase (GLX) |
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