Purification and Investigation of Physicochemical and Regulatory Properties of Homogeneous L-Lactate: Cytochrom c Oxidoreductase Obtained from the Nonsulfur Purple Bacterium Rhodovulum steppense
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L-Lactate: cytochrome c oxidoreductase activity was detected in cells of strain A-20s of the nonsulfur haloalkalophilic purple bacterium Rhodovulum steppense. An electrophoretically homogeneous preparation of the enzyme was obtained by purification. The enzyme had a specific activity of 4.75 U/mg protein, a 81.9-fold purification degree, and a 2.2% yield. The kinetic and physicochemical characteristics were determined. The value of the Michaelis constant with lactate was 15 μM. The temperature optimum for the studied enzyme was 31°C; optimum of pH was 8.2. It was found that the enzyme was a homodimer with a molecular weight of ~140 kDa; the mass of individual subunit was 68 kDa.
KeywordsL-lactate: cytochrome c oxidoreductase haloalkalophilic purple bacteria ion exchange chromatography gel chromatography subunit structure electrophoresis the Michaelis constant Rhodovulum steppense
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- 7.Masuda, S., Hori, K., Maruyama, F., Res, S., Suqimoto, S., Yamamoto, N., Mori, H., Yamada, T., Sato, S., Tabata, S., Ohta, H., and Kurokawa, K., Genome Announcement, 2013, vol. 1, no. 3. e00577–13.Google Scholar
- 8.Nagao, N., Hirose, Y., Misawa, N., Umekage, S., and Kikuchi, Y., Genome Announcement, 2015, vol. 3, no. 2. e00388–15.Google Scholar
- 14.Larchenkov, V.M., Sorokina, T.V., Akhmed, A.Kh., Tseluiko, Zh.A., Falaleeva, M.I., and Eprintsev, A.T., Sorbts. Khromatogr. Prots. (Voronezh), 2015, vol. 15, no. 5, pp. 714–719.Google Scholar
- 18.Lakin, G.F., Biometriya (Biometry), Moscow: Vysshaya shkola, 1990.Google Scholar