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Plant Physiology 65:229-233 (1980)
© 1980 American Society of Plant Biologists

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Presence in Dry Pea Cotyledons of Soluble Succinate Dehydrogenase That Is Assembled into the Mitochondrial Inner Membrane during Seed Imbibition 1

Natsuki Nakayama, Iwao Sugimoto2 and Tadashi Asahi

Laboratory of Biochemistry, Faculty of Agriculture, Nagoya University, Chikusa, Nagoya 464, Japan

Succinate dehydrogenase (succinate: phenazine methosulfate oxidoreductase, EC 1.3.99.1) activity in crude mitochondrial fraction from pea (var. Alaska) cotyledons increased during seed imbibition to reach a maximum after about 12 hours. The increase was not inhibited by either cycloheximide or D(-)threo-chloramphenicol. The postmicrosomal fraction from dry cotyledons, but not that from fully imbibed ones, contained a soluble form of succinate dehydrogenase. The soluble enzyme was partially purified by ammonium sulfate fractionation and diethylaminoethyl-cellulose and Sepharose 6B column chromatography. The enzyme showed no succinate-coenzyme Q oxidoreductase activity and had a molecular mass of about 100,000 daltons. The soluble enzyme seemed to differ only slightly from succinate dehydrogenase solubilized from the mitochondrial inner membrane from fully imbibed cotyledons by a detergent. It is proposed that the soluble succinate dehydrogenase is associated with an inert mitochondrial inner membrane in dry cotyledons to form an active one during seed imbibition.

2 Present address: Laboratory of Food Science and Technology (Animal Products), Faculty of Agriculture, Nagoya University.

1 This work was supported in part by Grants-in-Aid 311908 and 334037 for Scientific Research from the Ministry of Education, Science and Culture of Japan.






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Copyright © 1980 by the American Society of Plant Biologists