Changes in Properties of Succinate Dehydrogenase during Senescence of Pea Cotyledons

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Comparisons were made between succinate dehydrogenases (EC 1.3.99.1) from 1-day-old and 5-day-old pea cotyledons. The enzyme was loosely bound to the mitochon-drial inner membrane in 5-day-old cotyledons, but tightly in 1-day-old cotyledons. In addition, the enzyme partially purified from 5-day-old cotyledons was much more labile than that from 1-day-old cotyledons. Succinate rapidly inactivated partially purified succinate dehydrogenase from 1-day-old cotyledons, but not from 5-day-old cotyledons. Dithiothreitol caused a change in the charge of the enzyme protein from either 1- or 5-day-old cotyledons, only when succinate was present. The enzyme from 5-day-old cotyledons differed from the succinate-induced labile form of the enzyme from 1-day-old cotyledons in electrophoretic properties on a polyacrylamide gel. There was also a difference in the pattern of polyacrylamide gel electrophoresis between succinate dehydrogenases partially purified from 1- and 5-day-old cotyledons. The partially purified enzyme from either 1- or 5-day-old cotyledons in the presence of succinate had a molecular weight of 92,000. The molecular weight of the large subunit was suggested to be 65,000. The partially purified enzyme prepared from 1-day-old cotyledons in the absence of succinate was in a form with a molecular weight of 113,000.
日本植物生理学会の論文