Abstract
The reconstitution of pyruvate decarboxylase has been studied kinetically in thepresence of several concentrations of thiamine pyrophosphate (TPP) and Mn2+. The Km for TPP determined graphically was decreased by increasing Mn2+ concentration, while Vmax was almost unchanged. The values of Kms for Mn2+ and Vmax, were affected in mixed manner by the amount of TPP.The significance of Kms thus determined is discussed and the values are compared to that determined in transketolase.
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