Physicochemical, catalytic, and regulatory properties of malate dehydrogenase from Rhodovulum steppense bacteria, strain A-20s.
In: Biology Bulletin, Jg. 41 (2014-11-01), Heft 6, S. 486-492
Online
academicJournal
Zugriff:
The physicochemical, regulatory, and kinetic properties of malate dehydrogenase (EC 1.1.1.37) from haloalkaliphilic purple nonsulfur Rhodovulum steppense bacteria, strain A-20s, were studied. The malate dehydrogenase (MDH) preparation with a specific activity of 3.775 ± 0.113 U/mg protein was obtained in an electrophoretically homogeneous state using multistep purification. Using homogenous preparations, the molecular weight and the Michaelis constant of the enzyme were determined; the effects of metal ions, the temperature effect, and the thermal stability of the MDH were studied. The dimer structure of the enzyme was demonstrated by DS-Na-electrophoresis. [ABSTRACT FROM AUTHOR]
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Physicochemical, catalytic, and regulatory properties of malate dehydrogenase from Rhodovulum steppense bacteria, strain A-20s.
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Autor/in / Beteiligte Person: | Eprintsev, A. ; Falaleeva, M. ; Parfenova, I. ; Lyashchenko, M. ; Kompantseva, E. ; Tret'yakova, A. |
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Zeitschrift: | Biology Bulletin, Jg. 41 (2014-11-01), Heft 6, S. 486-492 |
Veröffentlichung: | 2014 |
Medientyp: | academicJournal |
ISSN: | 1062-3590 (print) |
DOI: | 10.1134/S1062359014050033 |
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