Abstract
Publisher Summary This chapter describes the procedures for resolving thiamine pyrophosphate (TPP)-enzymes and the reconstitution of enzymes resolved for TPP and Mg 2+ . Pyruvate decarboxylase from yeast; transketolase from spinach, yeast, and rat liver; α-ketoglutarate dehydrogenase from pig heart muscle; and the enzyme systems catalyzing the phosphoroclastic split of pyruvate from Clostridium butyricum and Clostridium kluyveri , all seem to bind TPP in a nondissociating manner. α-Acetolactate synthetase from Aerobacter aerogenes and glyoxylate carboligase from Escherichia coli appear to be heterogeneous in that only part of each enzyme binds TPP irreversibly. Cofactors are bound in a reversible manner by pyruvate decarboxylase from wheat germ, pyruvate dehydrogenase from E. coli , diacetylmethyl-carbinol synthetase from Micrococcus ureae , pyruvate oxidase from E. coli , and pyruvate oxidase from Proteus vulgaris , and they are lost during purification of these enzymes. The different methods that have been used for the cofactor resolution of TPP-enzymes from several sources are described in the chapter.
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