Title: Enzymic assay of pyridoxal phosphate using tyrosine apodecarboxylase and tyrosine-1-14C
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.
Publication Year: 1968
Publication Date: 1968-12-01
Language: en
Type: article
Indexed In: ['crossref', 'pubmed']
Access and Citation
Cited By Count: 44
AI Researcher Chatbot
Get quick answers to your questions about the article from our AI researcher chatbot