Jun 1, 1975

Purification and characterization of pyruvate decarboxylase from sweet potato roots

Journal of Biochemistry
K Oba, I Uritani

Abstract

Pyruvate decarboxylase [2-oxo acid carboxy-lyase, EC 4.1.1.1] was isolated from sweet potato roots and was partially purified from healthy and diseased tissues. There was no appreciable difference in properties between the enzymes from healthy and diseased tissues. The molecular weight of the enzyme was found to be 240,000 by polyacrylamide gel electrophoresis. Since sodium dodecyl sulfate polyacrylamide gel electrophoresis gave a molecular weight of 60,000 for the monomeric form of the enzyme, it is likely that sweet potato pyruvate decarboxylase contains 4 single polypeptide chains. The optimal pH of the decarboxylation reaction was 6.1--6.6. The Lineweaver-Burk double reciprocal plot curved upward, and the Hill coefficient was more than 1, with low concentrations of pyruvate. The enzyme was localized in the cytosol fraction. The activity of the enzyme increased in response to black-rot fungus infection, but decreased in response to cutting.

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Mentioned in this Paper

Mycoses
Ipomoea batatas
Enzymes, antithrombotic
Pyruvate Measurement
Lyase
Carboxy-Lyases
Pyruvate
Enzymes for Treatment of Wounds and Ulcers
Purification Aspects
Sweet potato allergenic extract

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