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.

中文翻译：

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均质状态下玉米盾构琥珀酸脱氢酶组成型同工酶的纯化及其特性研究

摘要

改良的四阶段纯化方案的使用使我们能够在种子发芽的后期从玉米（Sea mays L.）盾片获得组成均一的琥珀酸脱氢酶组成型的电泳均质制剂。已经确定同工酶的四级结构显着不同。因此，结果表明琥珀酸脱氢酶1为异四聚体，琥珀酸脱氢酶2为异二聚体。发现它们的主要催化和动力学特征也不同，特别是由于它们对底物（琥珀酸酯）的亲和力和催化反应的最佳pH值。琥珀酸脱氢酶2的特征是增强了对特定抑制剂丙二酸酯的抗性。