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.
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Eprintsev, A.T., Falaleeva, M.I., Stepanova, I.Y. et al. Purification and Physicochemical Properties of Malate Dehydrogenase from Bacteria of the Genus Beggiatoa . Biochemistry (Moscow) 68, 172–176 (2003). https://doi.org/10.1023/A:1022693211134
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DOI: https://doi.org/10.1023/A:1022693211134