Physicochemical,catalytic, and regulatory properties of malate dehydrogenase from Rhodovulum steppense bacteria,strain A-20s |
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| Authors: | A T Eprintsev M I Falaleeva I V Parfenova M S Lyashchenko E I Kompantseva A Yu Tret’yakova |
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| Institution: | 1. Voronezh State University, Universitetskaya pl. 1, Voronezh, 394006, Russia
2. Vinogradskii Institute of Microbiology, Russian Academy of Sciences, pr. 60-letiya Oktyabrya 7/2, Moscow, 117811, Russia
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| Abstract: | The physicochemical, regulatory, and kinetic properties of malate dehydrogenase (EC 1.1.1.37) from haloalkaliphilic purple nonsulfur Rhodovulum steppense bacteria, strain A-20s, were studied. The malate dehydrogenase (MDH) preparation with a specific activity of 3.775 ± 0.113 U/mg protein was obtained in an electrophoretically homogeneous state using multistep purification. Using homogenous preparations, the molecular weight and the Michaelis constant of the enzyme were determined; the effects of metal ions, the temperature effect, and the thermal stability of the MDH were studied. The dimer structure of the enzyme was demonstrated by DS-Na-electrophoresis. |
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