Eprintsev A T, Falaleeva M I, Stepanova I Yu, Parfenova N V
Department of Plant Biochemistry and Physiology, Voronezh State University, Voronezh, 394693, Russia.
Biochemistry (Mosc). 2003 Feb;68(2):172-6. doi: 10.1023/a:1022693211134.
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.
从以有机营养和无机营养方式生长的硫细菌纤细贝日阿托氏菌菌株D - 402以及有机营养细菌白色贝日阿托氏菌中纯化出了比活性为每毫克蛋白质20 - 24单位的均一苹果酸脱氢酶(MDH)。在有机营养条件下生长的纤细贝日阿托氏菌菌株D - 402和白色贝日阿托氏菌的MDH是亚基分子量为40 kD的同型二聚体。在无机营养条件下生长的纤细贝日阿托氏菌菌株D - 402中形成了四聚体MDH。纤细贝日阿托氏菌D - 402的二聚体和四聚体形式的MDH在动力学性质上表现出一些差异。