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Plant and Cell Physiology, 1992, Vol. 33, No. 4 489-491
© 1992

Short Communication

Properties of the Dicyclohexylcarbodiimide-Binding Subunit of Cytochrome c Oxidase from Sweet Potato

Tsuyoshi Nakagawa1, Masayoshi Maeshima2, Hideyo Muto and Tadashi Asahi3

Laboratory of Biochemistry, School of Agriculture, Nagoya University Chikusa, Nagoya, 464-01 Japan

1To whom correspondence should be addressed.

Subunit IV of cytochrome c oxidase from sweet potato was bound with dicyclohexylcarbodiimide and synthesized in isolated mitochondria. Thus, this subunit corresponds to subunit HI of the analogous mammalian and fungal enzymes. Subunit IV was a mixture of two polypeptides (subunits IVa and IVb) which differed slightly in structure.

1Present address: Research Institute of Molecular Genetics, Shimane University, Matsue, 690 Japan.

2Present address: Institute of Low Temperature Science, Hokkaido University, Sapporo, 060 Japan.

(Received December 18, 1991; Accepted February 26, 1992)
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