Abstract
A new approach for determination of pyridoxal phosphate in biological material is reported. The principle of the method is based on the decarboxylation reaction of l-tyrosine catalyzed by l-tyrosine decarboxylase ( l-tyrosine carboxy-lyase, EC 4.1.1.25) in the presence of pyridoxal phosphate. l-Tyrosine-1- 14C was used as the substrate and the rate of decarboxylation reaction was followed by a decrease of the radioactivity of the reaction mixture. Preparation of cell-free and pyridoxal phosphate free tyrosine apodecarboxylase was described. By this method, pyridoxal phosphate can be assayed for quantities of less than 5 ng. Concentrations of pyridoxal phosphate in whole blood, brains, and livers from both pyridoxine deficient and normal rats were also reported.
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