An enzymatic fluorometric assay to quantitate plasma pyridoxal 5'-phosphate (PLP) is described. PLP is preincubated for 30 min with purified tyrosine decarboxylase apoenzyme (TDA) in acetate buffer and is then incubated with L-tyrosine for 60 min. The decarboxylated metabolite, tyramine, is extracte
A new enzymatic method for pyridoxal-5-phosphate determination
โ Scribed by Y. S. Shin-Buehring; R. Rasshofer; W. Endres
- Publisher
- Springer
- Year
- 1981
- Tongue
- English
- Weight
- 154 KB
- Volume
- 4
- Category
- Article
- ISSN
- 0141-8955
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
A new enzymatic method for the synthesis of ['4C]pyridoxal 5'-phosphate is presented. [ r4C]Pyridoxal 5'-phosphate was synthesized from [ "C]pyridoxine through the successive actions of pyridoxal kinase and pyridoxamine 5'-phosphate oxidase in a reaction mixture containing ATP, ['4C]pyridoxine. and
Wood et al. (1) investigated a tryptophanase preparation obtained from Escherichiu coli, and found that it converted tryptophan to indole, pyruvate, and ammonia, and that pyridoxal phosphate was needed as a coenzyme for the reaction. Utilizing this reaction, Wada et nl. (2) determined the amount of
Pyridoxal Y-phosphate was synthesized by first oxidizing [Wlpyridoxine to [Wlpyridoxal with MnOp ["C]Pyridoxal, isolated by cation-exchange chromatography, was then reacted with ATP in the presence of rat liver pyridoxal kinase to form ["C]pyridoxal Y-phosphate. The rat liver enzyme was used instead
An assay for determining the concentration of pyridoxal Y-phosphate in plasma from 0.4 ml whole blood is reported. The assay consists of incubating deproteinized plasma with o-setine apodehydratase from Escherichia cob' in 0.5 M N-2-hydroxyethylpipetazine-N'-3-propesulfonic acid, pH 7.8, at 37ยฐC for