Differences in the Thermostability and Subunit Species of Cytochrome c Oxidase among Tissues
スポンサーリンク
概要
- 論文の詳細を見る
Cytochrome c oxidase associated with the mitochondrial inner membrane of the overground or underground organs of mung bean was more stable at 40-55℃ than that of the corresponding organs of pea. In both plants, the enzyme in the overground organs was more resistant to heat inactivation than that in the underground organs. When the enzyme was solubilized and partially purified from mung bean hypocotyls or roots, the enzyme became more labile and was stabilized by exogenous phospholipid. The enzyme partially purified from mung bean hypocotyls was more resistant to inactivation than that from its roots either in the presence or absence of phos-pholipid. A subunit (subunit Va) of cytochrome c oxidase in mung bean hypocotyls differed im-munologically from that in the roots. We propose that at least in mung bean, a nuclear-encoded subunit of cytochrome c oxidase is synthesized tissue-specifically, which may cause the difference in the thermostability of the enzyme.
- 日本植物生理学会の論文
著者
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Maeshima Masayoshi
Graduate School of Bioagricultural Sciences, Nagoya University
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MAESHIMA Masayoshi
Laboratory of Cell Dynamics, Graduate School of Bioagricultural Sciences, Nagoya University
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Asahi Tadashi
Laboratory of Biochemistry, School of Agriculture, Nagoya University
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Nakagawa Tsuyoshi
Laboratory Of Biochemistry School Of Agriculture Nagoya University:(present)research Institute Of Me
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Maeshima Masayoshi
Laboratory Of Biochemistry Graduate School Of Bioagricultural Sciences Nagoya University
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Maeshima M
Laboratory Of Cell Dynamics Graduate School Of Bioagricultural Sciences Nagoya University
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Asahi T
Fukui Prefectural Univ. Fukui Jpn
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Asahi Tadashi
Laboratory Of Biochemistry Faculty Of Agriculture Nagoya University
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Maeshima Masayoshi
Laboratory Cell Dynamics Graduate School Of Bioagricultural Sciences Nagoya University
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Asahi Tadashi
Laboralory Of Biochemistry Faculty Of Agriculture Nagoya University
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