title: Purification and physicochemical properties of malate dehydrogenase from bacteria of the genus Beggiatoa.
abstract: 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.
authors.affiliation: Department of Plant Biochemistry and Physiology, Voronezh State University, Voronezh, 394693, Russia. bsbc366@main.vsu.ru
authors.forename: A T
authors.initials: AT
authors.lastname: Eprintsev
authors.forename: M I
authors.initials: MI
authors.lastname: Falaleeva
authors.forename: I Yu
authors.initials: IY
authors.lastname: Stepanova
authors.forename: N V
authors.initials: NV
authors.lastname: Parfenova
mesh_terms: 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*
chemical_list: D021122:Protein Subunits; D008291:Malate Dehydrogenase