Physicochemical and catalytic properties of NAD+- dependent malate dehydrogenase isoforms from maize mesophyll
- 作者: Eprintsev A.T.1, Gataullina M.O.1, Lyashchenko M.S.1
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隶属关系:
- Voronezh State Utiversity
- 期: 卷 52, 编号 4 (2016)
- 页面: 366-370
- 栏目: Article
- URL: https://journals.rcsi.science/0003-6838/article/view/151948
- DOI: https://doi.org/10.1134/S0003683816040049
- ID: 151948
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详细
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.
作者简介
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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