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Hemoglobin
international journal for hemoglobin research
Volume 5, 1981 - Issue 3
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Original Article

Acetaldehyde-Dependent Changes in Hemoglobin and Oxygen Affinity of Human Erythrocytes

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Pages 241-250 | Received 03 Jul 1980, Accepted 10 Oct 1980, Published online: 07 Jul 2009
 

Abstract

In the presence of acetaldehyde, metabolizing human erythrocytes accumulate an altered hemoglobin product showing chromatographic similarity to hemoglobin AIa or AIb. The adduct is stable to overnight dialysis with an intracellular half-life of about 5.5 days. Adduct formation is accompanied by proportional changes in cell oxygen affinity (decrease in P50 of 3 mm Hg/mM adduct). Little unaltered hemoglobin remains after overnight incubation in 15 mM acetaldehyde, with significant adduct formation and marked reduction of cell ATP occurring after prolonged incubation in as little as 0.5 mM acetaldehyde.

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