Equimolar concentrations of 2-deoxy-d-glucose inhibited anaerobic glycolysis of Ehrlich ascites tumor cells when either d-glucose or d-fructose was used as the substrate, glycolysis with the latter being more strongly inhibited. 2-Deoxy-d-glucose did not inhibit anaerobic glycolysis primarily at the monosaccharide transport level. Instead it was converted to 2-deoxy-d-glucose-6-phosphate by tumor hexokinase and the latter compound inhibited both phosphohexoisomerase and a further step in the Embden-Meyerhof pathway subsequent to phosphofructokinase action. The Michaelis-Menten constants of hexokinase suggest that 2-deoxy-d-glucose may also inhibit hexokinase action on d-fructose.

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This investigation was supported in part by American Cancer Society Institutional Grants Nos. 22-C and 22-D. The material was taken in part from a dissertation submitted to the Horace H. Rackham School of Graduate Studies by Marshall Nirenberg in partial fulfillment of the requirements for the degree of Doctor of Philosophy in the University of Michigan, 1957.

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©1958 American Association for Cancer Research.
1958
Cancer Research, Inc.