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Plant Physiology 70:1577-1581 (1982)
© 1982 American Society of Plant Biologists

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Articles

Succinate Dehydrogenase 1

A Partial Purification from Mung Bean Hypocotyls and Soybean Cotyledons

John J. Burke2, James N. Siedow and Donald E. Moreland

United States Department of Agriculture, Agricultural Research Service, North Carolina State University, Raleigh, North Carolina 27650, Department of Crop Science, North Carolina State University, Raleigh, North Carolina 27650, Department of Botany, North Carolina State University, Raleigh, North Carolina 27650, Botany Department, Duke University, Durham, North Carolina 27706

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.

2 Present Address: Plant and Soil Science Department, Texas Tech University, Lubbock, TX 79409.

1 Supported in part by a grant from the National Institute of General Medical Sciences (USPHS GM26095) to J. N. S. Cooperative investigation of the United States Department of Agriculture, Agricultural Research Service, North Carolina Agricultural Research Service, Raleigh, and Duke University, Durham, NC. Paper No. 8286 of the Journal Series of the North Carolina Agricultural Research Service at Raleigh 27650.






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Copyright © 1982 by the American Society of Plant Biologists