[Isoformes of Malate Dehydrogenase from Rhodovulum Steppense A-20s Grown Chemotrophically under Aerobic Condtions].
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.
A T
AT
Eprintsev
M I
MI
Falaleeva
M S
MS
Lyashchenko
M O
MO
Gataullinaa
E I
EI
Kompantseva
D000332:Aerobiosis; D008291:Malate Dehydrogenase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D020033:Protein Isoforms / Q000737:chemistry* / Q000378:metabolism; D021122:Protein Subunits / Q000737:chemistry*; D041903:Rhodovulum / Q000201:enzymology
D020033:Protein Isoforms; D021122:Protein Subunits; D008291:Malate Dehydrogenase