Abstract
The rate of enzymatic conversion of thiamine to thiamine pyrophosphate (TPP) provides a convenient means of determining thiamine pyrophosphokinase activity. For the estimation of TPP, pyruvate decarboxylase and transketolase, which are completely dependent on their coenzyme, are used. A radiometric procedure, which allows the direct measurement of TPP, is described in this chapter. The amount of labeled TPP formed in the reaction from labeled thiamine and adenosine triphosphate (ATP) is determined after separation from the reaction mixture by paper chromatography or by electrophoresis. The enzyme has been partially purified from brewers' yeast and liver. It has been detected in several animal tissues and in microorganisms. In Escherichia coli , it is located in the spheroplasts, whereas it is found exclusively (more than 99%) in the soluble fraction of rat erythrocytes and of rat liver cells.
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