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


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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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A. Eprintsev

Voronezh State Utiversity

编辑信件的主要联系方式.
Email: bc366@bio.vsu.ru
俄罗斯联邦, Voronezh, 394006

M. Gataullina

Voronezh State Utiversity

Email: bc366@bio.vsu.ru
俄罗斯联邦, Voronezh, 394006

M. Lyashchenko

Voronezh State Utiversity

Email: bc366@bio.vsu.ru
俄罗斯联邦, Voronezh, 394006

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