Isoformes of Malate Dehydrogenase from Rhodovulum Steppense A-20s Grown Chemotrophically under Aerobic Condtions
Eprintsev, A.T.; Falaleeva, M.I.; Lyashchenko, M.S.; Gataullinaa, M.O.; Kompantseva, E.I.
Prikladnaia Biokhimiia i Mikrobiologiia 52(2): 168-173
2016
ISSN/ISBN: 0555-1099 PMID: 27266245 Document Number: 690258
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 Rhodovulum steppense bacteria strain A-20s chemotropically 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.