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Plant and Cell Physiology, 1982, Vol. 23, No. 3 515-523
© 1982

Article

The Presence of Two Forms of Succinate Dehydrogenase in Sweet Potato Root Mitochondria1

Tsukaho Hattori and Tadashi Asahi

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

Succinate dehydrogenase was partially purified from sweet potato root tissue by solubilization of the enzyme from the submitochondrial particles, ammonium sulfate fractionation, and DEAE-cellulose column chromatography. Sweet potato succinate dehydrogenase existed in two forms; these were separated by disc polyacrylamide gel electrophoresis or by hydroxyapatite column chromatography. There was a difference in the electric charge of the molecule, but not in the molecular weights of the two forms. No difference was detected between the two forms of succinate dehydrogenase with respect to their Km values for succinate, pH-optimums and subunit compositions. The two subunits that make up the enzyme have molecular weights of about 26,000 and 65,000.

1 This work was supported in part by Grant-in-Aid 411308 for Scientific Research from the Ministry of Education, Science and Culture of Japan.

(Received November 28, 1981; Accepted February 17, 1982)
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