Inorganic pyrophosphate-glucose phosphotransferase activity associated with alkaline phosphatase of Escherichia coli.

@article{Anderson1967InorganicPP,
  title={Inorganic pyrophosphate-glucose phosphotransferase activity associated with alkaline phosphatase of Escherichia coli.},
  author={Wayne B. Anderson and Robert C. Nordlie},
  journal={The Journal of biological chemistry},
  year={1967},
  volume={242 1},
  pages={114-9}
}
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 E. coli enzyme was further characterized relative to catalytic properties. Adenosine 5’-phosphate, diphosphate, and triphosphate, cytidine 5… CONTINUE READING
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WOOD (Editor), Methods in enzymology

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