title: Succinate dehydrogenase : a partial purification from mung bean hypocotyls and soybean cotyledons.
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.
authors: United States Department of Agriculture, Agricultural Research Service, North Carolina State University, Raleigh, North Carolina 27650.
authors: J J
authors: JJ
authors: Burke
authors: J N
authors: JN
authors: Siedow
authors: D E
authors: DE
authors: Moreland