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(1991)
Malatdegidrogenaza vysshikh rastenii (Malate Dehydrogenase of Higher Plants), Voronezh: Izd
(1998)
Veroyatnost’ i statistika v biologii i khimii (Probability and Statistics in Biology and Chemistry)
(2007)
Glioksilatnyi tsik: universal'nyi mekhanizm adaptatsii?
(1964)
Society for the Study at the New York Academy of Medicine
(2005)
Ekspressiya i regulyatsiya fermentov glioksilatnogo tsikla (Expression and Regulation of Glyoxylate Cycle Enzymes)
Peroxisomal malate dehydrogenase (EC 1.1.1.37) with a specific activity of 533 U/mg (144-fold purification) and a yield of 5% was obtained in a homogeneous state by a purification scheme including sucrose gradient centrifugation from maize mesophyll. The Michaelis constants for the forward and reverse reactions were determined to be 11.6 mM and 256 μM, and the pH optimum was 9.5 and 9.0, respectively. Analysis of the molecular weight of the native enzyme and its subunits showed that the peroxisomal malate dehydrogenase was a homodimer. It was established that the isolated and purified isoform of the enzyme had a higher affinity for malate and NAD+ in comparison with the mitochondrial and cytoplasmic isoforms.
Applied Biochemistry and Microbiology – Springer Journals
Published: Jun 1, 2018
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