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Purification of Constitutive Isoenzymes of Succinate Dehydrogenase from Zea mays Scutellum in the Homogeneous State and the Study of Their Characteristics

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Abstract

The use of a modified, four-stage purification scheme allowed us to obtain electrophoretically homogeneous preparations of constitutive forms of succinate dehydrogenase from maize (Zea mays L.) scutellum in the late stages of seed germination. It has been established that the isoenzymes differed significantly in their quaternary structure. Thus, succinate dehydrogenase 1 turned out to be a heterotetramer, and succinate dehydrogenase 2 turned out to be a heteroterodimer. It was found that their main catalytic and kinetic characteristics also differed, in particular, by their affinity to the substrate (succinate) and the value of pH optimum of the catalyzed reaction. Succinate dehydrogenase 2 was characterized by enhanced resistance to a specific inhibitor—malonate.

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Funding

The work was financially supported by the Russian Science Foundation (project no. 19-14-00150).

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  1. Voronezh State University, 394018, Voronezh, Russia

    A. T. Eprintsev & D. N. Fedorin

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  1. A. T. Eprintsev
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  2. D. N. Fedorin
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Correspondence to A. T. Eprintsev.

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The authors declare that they have no conflict 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 T. Borisova

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Eprintsev, A.T., Fedorin, D.N. Purification of Constitutive Isoenzymes of Succinate Dehydrogenase from Zea mays Scutellum in the Homogeneous State and the Study of Their Characteristics. Appl Biochem Microbiol 56, 179–184 (2020). https://doi.org/10.1134/S0003683820020064

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