Abstract
Formaldehyde released during hydrolysis of calcium-chelator esters incorporated into cells blocks glycolysis in the human erythrocyte (Tiffert, T., García-Sancho, J. and Lew, V.L. (1984) Biochim. Biophys. Acta 773, 143-156). This blockade is due to the inhibition of glyceraldehyde-3-phosphate dehydrogenase by NAD+ depletion caused by enzymatic oxidation of formaldehyde coupled to NADH production. The addition of pyruvate to the incubation medium prevents or reverts ATP depletion.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphate / metabolism*
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Aminoquinolines / pharmacology*
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Erythrocytes / drug effects
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Erythrocytes / metabolism*
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Formaldehyde / pharmacology*
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Glyceraldehyde-3-Phosphate Dehydrogenases / metabolism
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Humans
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In Vitro Techniques
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NAD / metabolism
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Pyruvates / pharmacology*
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Pyruvic Acid
Substances
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Aminoquinolines
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Pyruvates
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NAD
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Formaldehyde
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Quin2-acetoxymethyl ester
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Pyruvic Acid
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Adenosine Triphosphate
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Glyceraldehyde-3-Phosphate Dehydrogenases