Pyruvic oxidase of pigeon breast muscle I. Purification and properties of the enzyme

Abstract

Pyruvate oxidation in bacterial extracts has been studied by several authors (l-7). Flavin-adenine dinucleotide, cocarboxylase, phosphate, and Mg⁺⁺ are required for activity in preparations from Lactobacillus delbrueck ii (l-3) and from Escherichia coli (5). The nature of the primary intermediates in these oxidations is not fully understood. Less is known about pyruvate oxidation in animal tissues. Stumpf et al. (8) were able to obtain a particulate preparation from pigeon breast muscle which catalyzed the oxidation of pyruvate to acetate and carbon dioxide. In the present series of papers, the further purification of this enzyme, its physicochemical properties, and the factors implicated in its activity are discussed.