Modifications of Purified Glucose-6-phosphate Dehydrogenase and other Enzymes by a Factor of Low Molecular Weight Abundant in Some Leukemic Cells

Highly purified platelet glucose-6-phosphate dehydrogenase (G6PD; D-glucose-6-phosphate:NADP+ 1-oxidoreductase, EC 1.1.1.49) can be modified in its isoelectric point and its molecular specific activity by extracts of some leukemic granulocytes. The ``G6PD modifying factors'' are relatively...

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Published in:Proceedings of the National Academy of Sciences - PNAS 1976-01, Vol.73 (1), p.77-81
Main Authors: Kahn, Axel, Boivin, Pierre, Rubinson, Henriette, Cottreau, Dominique, Marie, Joelle, Dreyfus, Jean-Claude
Format: Article
Language:English
Subjects:
Blood Platelets - enzymology
Chlorides
Dehydrogenases
Electrophoresis
Enzymes
Gels
Glucose-6-Phosphate Isomerase - metabolism
Glucosephosphate Dehydrogenase - analysis
Glucosephosphate Dehydrogenase - blood
Glucosephosphate Dehydrogenase - metabolism
Hydrogen-Ion Concentration
Isoelectric Focusing
Leukemia - blood
Leukemia - enzymology
Leukocytes
Phosphates
Phosphogluconate Dehydrogenase - metabolism
Platelets
Pyruvate Kinase - metabolism
Starches
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Summary:Highly purified platelet glucose-6-phosphate dehydrogenase (G6PD; D-glucose-6-phosphate:NADP+ 1-oxidoreductase, EC 1.1.1.49) can be modified in its isoelectric point and its molecular specific activity by extracts of some leukemic granulocytes. The ``G6PD modifying factors'' are relatively small molecules (molecular weight slightly under 5000), thermostable, dialyzable, and ultrafilterable. These molecules are destroyed by various endo- and exopeptidases and by serine enzymes present in crude extracts of leukocytes and commercial preparations of ribonuclease. The alterations of platelet G6PD due to the ``G6PD modifying factors'' are stable and not reversible by dialysis or further chromatography. The leukemic extracts which are able to modify G6PD also can modify the electrophoretic mobility and (or) the enzymatic activity of purified leukocyte pyruvate kinase, 6-phosphogluconate dehydrogenase, and glucosephosphate isomerase. The chemical nature of such modifications and their relationships with post-translational modifications which occur in leukemic or normal cells are discussed.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.73.1.77