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Purification and Some Kinetic Characteristics of Succinate Dehydrogenase Isoenzymes from Maize Leaves under Salt Stress

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Abstract

Highly purified succinate dehydrogenase (SDH) preparations were obtained using multistage purification. Ion-exchange chromatography on DEAE-Sephacel was the key step that allowed us to separate isoenzymes of the studied enzyme from maize leaves under normal conditions and under salt stress. The specific activity of the resulting SDH preparations ranged from 0.623 to 1.095 U/mg protein, with the yield ranging from 41.33 to 78.21%. Comparative analysis of the obtained Km values and the pH optimum of the obtained succinate dehydrogenase isoenzymes shows a slight decrease in the activity of isoenzymes obtained from seedlings incubated under salt stress. An increase in Km values indicates a decrease in the affinity for the substrate in these two isoenzymes, which may cause the transformation of metabolic reactions during cell adaptation to stress.

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Authors and Affiliations

  1. Voronezh State University, 394018, Voronezh, Russia

    A. T. Eprintsev, D. N. Fedorin & O. Kh. Flores Karo

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  1. A. T. Eprintsev
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  2. D. N. Fedorin
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  3. O. Kh. Flores Karo
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Correspondence to A. T. Eprintsev.

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The authors declare that they have no conflicts of interest. This article does not contain any studies involving animals or human participants performed by any of the authors.

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Translated by V. Mittova

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Eprintsev, A.T., Fedorin, D.N. & Karo, O.K. Purification and Some Kinetic Characteristics of Succinate Dehydrogenase Isoenzymes from Maize Leaves under Salt Stress. Appl Biochem Microbiol 58, 790–795 (2022). https://doi.org/10.1134/S0003683822060035

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  • DOI: https://doi.org/10.1134/S0003683822060035

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