Immunological Studies on ATPases in Mung Bean Hypocotyl Plasma Membrane : Proposal of the Presence of Two Molecular Species of ATPase
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概要
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ATPase in a highly purified plasma membrane fraction from mung bean hypocotyls was solubilized by lysolecithin and fractionated by glycerol density gradient centrifugation. Lysolecithin activated ATPase activity in the lower but not in the upper half of the activity peak after glycerol density gradient centrifugation. Antibody against maize root plasma membrane ATPase [Nagao et al. (1987) Plant Cell Physiol. 28: 1181] reacted to a 100-kDa polypeptide which was localized only at the lower half of the activity peak. Antibody against a 67-kDa polypeptide, which was proposed to be a subunit of a new type of ATPase in mung bean hypocotyl plasma membrane (Mito et al. the preceding paper), reacted only to its own antigen which was present mainly in the upper half of the activity peak. The activity peak fraction contained a low-molecular-mass pol-ypeptide binding N,N'-dicyclohexylcarbodiimide. We propose the presence in mung bean hypocotyl plasma membrane of two distinct ATPases which differ from each other in polypeptide constitution and in their response to lysolecithin.
- 日本植物生理学会の論文
著者
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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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Kimura Tetsuya
Laboratory of Applied Microbiology, Faculty of Bioresources, Mie University
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Kimura Tetsuya
Laboratory Of Biochemistry School Of Agriculture Nagoya University
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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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