Abstract
Abstract The chemical syntheses of mono- and dimethyl esters of riboflavin phosphate were accomplished by allowing riboflavin to react with the appropriate mono- and dimethylchlorophosphoric acids. Riboflavin monomethyl phosphate was found to be coenzymatically active with nicotinamide adenine dinucleotide phosphate-cytochrome c aporeductase, pyridoxine (or pyridoxamine) phosphate apooxidase, and glycolate apooxidase. Riboflavin phosphate esters of cellulose phosphate and diethylaminoethyl cellulose were prepared by reactions with riboflavin dichlorophosphate in pyridine; the corresponding derivative of cellulose was prepared by reaction with riboflavin phosphate and dicyclohexylcarbodiimide in pyridine. The riboflavin phosphate cellulose compounds were used to retain the riboflavin phosphate-dependent apoenzymes selectively during their chromatographic purification from extraneous protein. Extensive enrichment of glycolate apooxidase was achieved by chromatography on riboflavin phosphate cellulose.
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