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Physicochemical and catalytic properties of NAD+- dependent malate dehydrogenase isoforms from maize mesophyll

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Abstract

Malate dehyrogenase isoforms (46- and 70-fold purifications) with specific activities of the 640 and 990 U/mg protein were obtained in an electrophoretically homogeneous state from maize mesophyll. The physicochemical and catalytic properties of these isoforms were studied. 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 SDS-PAGE demonstrated that malate dehydrogenase isoforms have an oligomeric structure comprised of identical subunits. The first isoform with a molecular weight of 126.58 kDa is tetramer, and the second isoform with a molecular weight of 63.3 is dimer.

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Correspondence to A. T. Eprintsev.

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Original Russian Text © A.T. Eprintsev, M.O. Gataullina, M.S. Lyashchenko, 2016, published in Prikladnaya Biokhimiya i Mikrobiologiya, 2016, Vol. 52, No. 4, pp. 365–369.

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Eprintsev, A.T., Gataullina, M.O. & Lyashchenko, M.S. Physicochemical and catalytic properties of NAD+- dependent malate dehydrogenase isoforms from maize mesophyll. Appl Biochem Microbiol 52, 366–370 (2016). https://doi.org/10.1134/S0003683816040049

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  • DOI: https://doi.org/10.1134/S0003683816040049

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