Inorganic Pyrophosphate-Glucose Phosphotransferase Activity Associated with Alkaline Phosphatase of Escherichia coZi*

Abstract

Highly purified commercial alkaline phosphatase preparations from Escherichia coli have been shown to catalyze the transfer of a phosphoryl group of inorganic pyrophosphate to the hydroxyl group attached to carbon atom 6 of glucose. Phosphotransferase activity also was detected with relatively crude chicken intestinal alkaline phosphatase preparations. The… (More)

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@inproceedings{Anderson2003InorganicPP, title={Inorganic Pyrophosphate-Glucose Phosphotransferase Activity Associated with Alkaline Phosphatase of Escherichia coZi*}, author={Wayne F. Anderson and Robert C. Nordlie}, year={2003} }