Effectors of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase of rat liver.
- 22 Downloads
The lower Vmax of 6PGDH with respect to G6PDH and its higher sensitivity to inhibition by NADPH, suggest the existence of an imbalance between the two dehydrogenases of the pentose phosphate pathway in rat liver. Possible modulators of these activities, particularly in relation with the inhibition by NADPH in physiological conditions, have been investigated. The results suggest that in both cases the inhibition by NADPH is strictly isosteric and that the relative affinities for the reduced and oxidized forms of the pyridine nucleotide are unaffected by glutathion, the intermediates of the pentose phosphate shunt or some divalent ions.
KeywordsPhosphate Nucleotide Pyridine NADPH Physiological Condition
glucose-6-phosphate dehydrogenase (EC 126.96.36.199)
6-phosphogluconate dehydrogenase (EC 188.8.131.52)
Unable to display preview. Download preview PDF.
- 1.Sapag-Hagar, M., Lagunas, R. and Sols, A., 1973. Biochem. Biophys. Res. Commun. 50, 179–185.Google Scholar
- 2.Schofield. P. J. and Sols, A., 1976. Biochem. Biophys. Res. Commun. 71, 1313–1318.Google Scholar
- 3.Bergmeyer, H. U., 1970. Methods of Enzymatic Analysis, Vol. 2, 2nd ed. Academic Press, Inc. New York and London.Google Scholar
- 4.Lagunas, R., McLean, P. and Greenbaum, A. L., 1970. European J. Biochem. 15, 179–190.Google Scholar
- 5.Greenbaum, A. L., Gumaa, K. A, and McLean, P., 1971. Arch. Biochem. Biophys. 143, 617–663.Google Scholar
- 6.Taketa, K. and Pogell, B. M, 1966. J. Biol. Chem. 241, 720–726.Google Scholar
- 7.Kawaguchi, A. and Bloch, K, 1974. J. Biol. Chem. 249, 5793–5800.Google Scholar
- 8.Eggleston, L. V. and Krebs, H. A., 1974. Biochem. J. 138, 425–435.Google Scholar