Succinate dehydrogenase. A partial purification from mung bean hypocotyls and soybean cotyledons [Vigna radiata, Glycine max, isolation procedure]

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...

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Bibliographic Details
Published in:Plant physiology (Bethesda) 1982-12, Vol.70 (6), p.1577-1581
Main Authors: Burke, John J., Siedow, James N., Moreland, Donald E.
Format: Article
Language:English
Subjects:
Cotyledons
Dehydrogenases
Enzymes
Gels
Glycine max
Malonates
Mitochondria
Phosphates
Solubilization
Soybeans
succinate dehydrogenase
Sulfates
Vigna radiata
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Summary: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.
ISSN:0032-0889
1532-2548
DOI:10.1104/pp.70.6.1577