Succinate Dehydrogenase

Abstract
A procedure was developed for the partial purification of succinate dehydrogenase from mung bean (V. radiata L.) hypocotyls and soybean (G. max [L] Merr. cv. Ransom) cotyledons. The procedure utilized a Triton X-100 extraction followed by ammonium sulfate precipitation. The final fraction was enriched in 2 polypeptides with approximate MW of 67,000 and 30,000 daltons, exhibited a pH optima of 7.0-7.5, contained a b-type cytochrome and exhibited the characteristic ferredoxin-type and high potential Fe-S protein-type EP signals reported for the Fe-S centers of mammalian succinate dehydrogenase. Inhibition constants of 1.15 and 24.6 .mu.M for oxaloacetate and malonate, respectively, were obtained.