Abstract
A method has been developed for the measurement of red cell pyridoxine (pyridoxamine) phosphate oxidase activity. The more stable substrate, pyridoxamine phosphate, was incubated with a red cell haemolysate and the product pyridoxal phosphate was measured by Lactobacillus casei microbiological assay. A wide range of oxidase activities was found in control subjects (6–136 ng pyridoxal phosphate/g Hb × 10 −2). There is a close correlation between the rate of conversion of pyridoxine to pyridoxal phosphate in whole blood and the oxidase activity. There was a marked increase in both after oral riboflavin. These results suggest that the oxidase plays a large part in the regulation of vitamins B-6 metabolism in red cells.
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