Isoformes of Malate Dehydrogenase from Rhodovulum Steppense A-20s Grown Chemotrophically under Aerobic Conditions


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Abstract

Three malate dehydrogenase isoforms (65-, 60-, and 71-fold purifications) with specific activities of 4.23, 3.88, and 4.56 U/mg protein were obtained in an electrophoretically homogenous state from Rhodоvulum steppense bacteria strain A-20s chemotrophically grown under aerobic conditions. The physicochemical and kinetic properties of malate dehydrogenase isoforms were determined. The molecular weight and the Michaelis constants were determined; the effect of hydrogen ions on the forward and reverse MDH reaction was studied. The results of the study demonstrated that the enzyme consists of subunits; the molecular weight of subunits was determined by SDS-PAGE.

About the authors

A. T. Eprintsev

Voronezh State University

Author for correspondence.
Email: bc366@bio.vsu.ru
Russian Federation, Voronezh, 394006

M. I. Falaleeva

Voronezh State University

Email: bc366@bio.vsu.ru
Russian Federation, Voronezh, 394006

M. S. Lyashchenko

Voronezh State University

Email: bc366@bio.vsu.ru
Russian Federation, Voronezh, 394006

M. O. Gataullina

Voronezh State University

Email: bc366@bio.vsu.ru
Russian Federation, Voronezh, 394006

E. I. Kompantseva

Winogradsky Institute of Microbiology

Email: bc366@bio.vsu.ru
Russian Federation, Moscow, 117811

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