Pyrophosphate glucose phosphotransferase

AlO. Arion, E. J., and Nordlie, R. C., Liver microsomal glucose-6-phosphatase, inorganic pyrophosphatase, and pyrophosphate-glucose-phosphotransferase. II. Kinetic studies. J. Biol. Chem. 239, 2752-2757 (1964). 

Stetten, M. R., and Burnett, F. R., 1966, Activation of rat liver microsomal glucose-6-phosphatase, inorganic pyrophosphatase and inorganic pyrophosphate-glucose phosphotransferase by hydroxyl ion, Biochim. Biophys. Acta 128 344. 

Pyrophosphate-glucose and nucleotide-glucose phosphotransferase activities exhibit maximal activity at pH 4.5 in untreated microsomal preparations or homogenates, and at pH 5.5-5.7 after detergent treatment and/or partial purification of the enzyme. Typical activity-pH profiles obtained with microsomal preparations from normal control, diabetic, and cortisone-treated animals, without and with supplemental detergent added, are presented in Fig. 2. 

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