Abstract
Abstract The phenylalanine hydroxylase cofactor from Pseudomonas species (ATCC 11299a) has been purified. The techniques used included dialysis, Florisil chromatography, carboxymethyl Sephadex chromatography, and paper chromatography with butyl alcohol-acetic acid-H2O as solvent. After oxidation of the purified material, several pteridines were isolated. The major component was shown to be 2-amino-4-hydroxy - 6 -(l - threotrihydroxypropyl) pteridine, l - threoneopterin. Also present were 6-carboxypterin, pterin, and xanthopterin. Some evidence was also obtained for the presence of erythroneopterin and a cyclic phosphate of neopterin. The observations suggest that the phenylalanine hydroxylase cofactor from Pseudomonas is reduced l-threoneopterin.
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