Purification and physicochemical properties of malate dehydrogenase from bacteria of the genus Beggiatoa.
Homogeneous malate dehydrogenase (MDH) with a specific activity of 20-24 units per mg protein was purified from the sulfur bacterium Beggiatoa leptomitiformis strain D-402 grown organotrophically and lithotrophically and from the organotrophic bacterium Beggiatoa alba. MDHs from the B. leptomitiformis strain D-402 grown under organotrophic conditions and from B. alba are homodimers with the subunit molecular weight of 40 kD. Tetrameric MDH is formed in B. leptomitiformis strain D-402 grown under lithotrophic conditions. The dimeric and tetrameric forms of MDH from B. leptomitiformis D-402 display some differences in kinetic properties.
Eprintsev
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Department of Plant Biochemistry and Physiology, Voronezh State University, Voronezh, 394693, Russia. bsbc366@main.vsu.ru
Falaleeva
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Stepanova
I Yu
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Parfenova
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NV
D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D008291:Malate Dehydrogenase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D008970:Molecular Weight; D021122:Protein Subunits; D041962:Thiotrichaceae / Q000201:enzymology*
D021122:Protein Subunits; D008291:Malate Dehydrogenase