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Molecular and Cellular Biochemistry

, Volume 17, Issue 3, pp 147–149 | Cite as

Effectors of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase of rat liver.

  • Ana Maria Gonzalez
  • Rosario Lagunas
General Articles

Summary

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.

Keywords

Phosphate Nucleotide Pyridine NADPH Physiological Condition 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Abbreviations

G6PDH

glucose-6-phosphate dehydrogenase (EC 1.1.1.49)

6PGDH

6-phosphogluconate dehydrogenase (EC 1.1.1.44)

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Copyright information

© Dr. W. Junk b.v. Publishers 1977

Authors and Affiliations

  • Ana Maria Gonzalez
    • 1
  • Rosario Lagunas
    • 1
  1. 1.Instituto de Enzimología del Consejo Superior de Investigaciones CientíficasFacultad de Medicina de la Universidad AutónomaMadrid-34Spain

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