[Isolation, purification, and properties of malate dehydrogenases from sulfur bacteria Beggiatoa leptomitiformis].
Malate dehydrogenase (E.C. 1.1.1.37) from bacterium Beggiatoa leptomitiformis was isolated and purified 123 times using a five-step purification procedure including the enzyme extraction, ammonium sulfate protein fractionation, gel filtration, ion exchange chromatography, and gel chromatography. The enzyme was homogenous according to the electrophoresis data; its activity was 20.43 U/mg proteins. This malate dehydrogenase is a homotetramer (Mr = 172 kDa). The catalytic and thermodynamic properties, as well as the analysis of the published data suggest that the tetrameric structure of the enzyme allows it to participate in constructive metabolism supplying the cell with organic acids as a source of carbon.
Eprintsev
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AT
Voronezh State University, Universitetskaya pl. 1, Voronezh, 394006 Russia.
Falaleeva
M I
MI
Stepanova
I Iu
IIu
Parfenova
N V
NV
Zuzu
M
M
D004591:Electrophoresis, Polyacrylamide Gel; D008291:Malate Dehydrogenase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D011487:Protein Conformation; D013379:Substrate Specificity; D041962:Thiotrichaceae / Q000201:enzymology*
D008291:Malate Dehydrogenase