| Autor: |
Eprintsev AT, Falaleeva MI, Lyashchenko MS, Gataullinaa MO, Kompantseva EI |
| Jazyk: |
ruština |
| Zdroj: |
Prikladnaia biokhimiia i mikrobiologiia [Prikl Biokhim Mikrobiol] 2016 Mar-Apr; Vol. 52 (2), pp. 168-73. |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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