Abstract
THE red cell is an active site for the conversion of pyridoxine to physiological forms of vitamin B6. Pyridoxine phosphate is first formed by a kinase and then converted to pyridoxal phosphate by an oxidase, followed by dephosphorylation to pyridoxal, the form which is released into plasma1. In a large proportion of the patients with homozygous or heterozygous β-thalassaemia whom we have studied, there was a much reduced in vitro rate of red-cell conversion of pyridoxine, a familial characteristic inherited separately from thalassaemia, and also found in some haematologically normal subjects2–4. This rate of conversion, whether reduced or normal, is increased by incubation of blood with riboflavin4, possibly through synthesis in the red cell of flavin mononucleotide (FMN) from riboflavin5, which then stimulates the pyridoxine phosphate oxidase6, a flavoprotein7. In order to study the in vivo effect on red-cell metabolism of B6, riboflavin was administered to one of the haematologically normal subjects with a greatly reduced red-cell conversion rate of pyridoxine. The rate increased to normal within 3 week. Here we report the details of this study.
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ANDERSON, B., SAARY, M., STEPHENS, A. et al. Effect of riboflavin on red-cell metabolism of vitamin B6. Nature 264, 574–575 (1976). https://doi.org/10.1038/264574a0
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DOI: https://doi.org/10.1038/264574a0
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