Isoformes of Malate Dehydrogenase from Rhodovulum Steppense A-20s Grown Chemotrophically under Aerobic Conditions
- Authors: Eprintsev A.T.1, Falaleeva M.I.1, Lyashchenko M.S.1, Gataullina M.O.1, Kompantseva E.I.2
-
Affiliations:
- Voronezh State University
- Winogradsky Institute of Microbiology
- Issue: Vol 52, No 2 (2016)
- Pages: 138-142
- Section: Article
- URL: https://journal-vniispk.ru/0003-6838/article/view/151862
- DOI: https://doi.org/10.1134/S0003683816020058
- ID: 151862
Cite item
Abstract
Three malate dehydrogenase isoforms (65-, 60-, and 71-fold purifications) with specific activities of 4.23, 3.88, and 4.56 U/mg protein were obtained in an electrophoretically homogenous state from Rhodоvulum steppense bacteria strain A-20s chemotrophically grown under aerobic conditions. The physicochemical and kinetic properties of malate dehydrogenase isoforms were determined. The molecular weight and the Michaelis constants were determined; the effect of hydrogen ions on the forward and reverse MDH reaction was studied. The results of the study demonstrated that the enzyme consists of subunits; the molecular weight of subunits was determined by SDS-PAGE.
About the authors
A. T. Eprintsev
Voronezh State University
Author for correspondence.
Email: bc366@bio.vsu.ru
Russian Federation, Voronezh, 394006
M. I. Falaleeva
Voronezh State University
Email: bc366@bio.vsu.ru
Russian Federation, Voronezh, 394006
M. S. Lyashchenko
Voronezh State University
Email: bc366@bio.vsu.ru
Russian Federation, Voronezh, 394006
M. O. Gataullina
Voronezh State University
Email: bc366@bio.vsu.ru
Russian Federation, Voronezh, 394006
E. I. Kompantseva
Winogradsky Institute of Microbiology
Email: bc366@bio.vsu.ru
Russian Federation, Moscow, 117811
Supplementary files
