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. 1982 Dec;70(6):1577-81.
doi: 10.1104/pp.70.6.1577.

Succinate dehydrogenase : a partial purification from mung bean hypocotyls and soybean cotyledons

J J Burke  1 , J N Siedow, D E Moreland
Affiliations

Succinate dehydrogenase : a partial purification from mung bean hypocotyls and soybean cotyledons

J J Burke et al. Plant Physiol. 1982 Dec.

Abstract

A procedure was developed for the partial purification of succinate dehydrogenase from mung bean (Vigna radiata L.) hypocotyls and soybean (Glycine max [L] Merr. v. Ransom) cotyledons. The procedure utilized a Triton X-100 extraction followed by ammonium sulfate precipitation. The final fraction was enriched in two polypeptides with approximate molecular weights of 67,000 and 30,000 daltons, exhibited a pH optima of 7.0 to 7.5, contained a b-type cytochrome, and exhibited the characteristic ferredoxin-type and high potential iron-sulfur protein-type electron paramagnetic resonance signals reported for the iron-sulfur centers of mammalian succinate dehydrogenase. Inhibition constants of 1.15 and 24.6 micromolar for oxaloacetate and malonate, respectively, were obtained.

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