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. 1982 Dec;70(6):1577–1581. doi: 10.1104/pp.70.6.1577

Succinate Dehydrogenase 1

A Partial Purification from Mung Bean Hypocotyls and Soybean Cotyledons

John J Burke 1,2,3,4,2, James N Siedow 1,2,3,4, Donald E Moreland 1,2,3,4
PMCID: PMC1065933  PMID: 16662722

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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