To test the antisickling activity of pyridoxal, we compared the oxygen affinity and the percent sickling at low PO2 of untreated erythrocytes with values for cells from the same blood sample incubated with pyridoxal, glyceraldehyde, or pyridoxine. Pyridoxal increased oxygen affinity much more than glyceraldehyde. 20 mM pyridoxal and glyceraldehyde had equivalent antisickling activity. At PO2 levels above 20 mm Hg, both agents reduced sickling to less than 2%. In samples examined by electron microscopy, pyridoxal reduced the percent sickled cells and the percent cells that contain hemoglobin S fibers by the same amount (from 74 to 3%). Pyridoxine had no effect on oxygen affinity or sockling. Pyridoxal reacts with intracellular hemoglobin to increase oxygen affinity, which inhibits hemoglobin S polymerization and sickling.
J A Kark, M P Kale, P G Tarassoff, M Woods, L S Lessin
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The Journal of Nutritional Biochemistry | 1997 |
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J Stuart, CS Johnson |
Baillière's Clinical Haematology | 1987 |
Covalent binding of glutathione to hemoglobin. I. Inhibition of hemoglobin S polymerization
MC Garel, C Domenget, J Caburi-Martin, C Prehu, F Galacteros, Y Beuzard |
The Journal of biological chemistry | 1986 |
Pyridoxal phosphate as an antisickling agent in vitro
JA Kark, PG Tarassoff, R Bongiovanni |
Journal of Clinical Investigation | 1983 |
Schiff base adducts of glyceraldehyde with hemoglobin. Differences in the Amadori rearrangement at the alpha-amino groups
AS Acharya, LG Sussman, JM Manning |
The Journal of biological chemistry | 1983 |
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R Seetharam, JM Manning, AS Acharya |
The Journal of biological chemistry | 1983 |
A rapid fluorometric assay for erythrocyte pyridoxal kinase
JA Kark, MJ Haut, CU Hicks, CT McQuilkin, RD Reynolds |
Biochemical Medicine | 1982 |
The Molecular Basis of Mutant Hemoglobin Dysfunction
DR Harkness |
The Molecular Basis of Mutant Hemoglobin Dysfunction | 1981 |