A purification of freshly reduced tetrahydrofolate by column chromatography has resulted in the separation of the moee active hydroxylase cofactor fraction from authentic tetrahydrofolate. In the present study, the purification of the two fractions is described and their roles as phenylalanine and tyrosine hydroxylase cofactors in previously used mixtures are compared. The moee active fraction has been characterized by physical, chemical, and enzymatic methods as 2-amino-4-hydroxy-6-methyltetrahydropterin. This very active unconjugated reduced pterin is produced in small amounts by the degradation of tetrahydrofolate during catalytic reduction.
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