Partial Purification and Characterization of An ATPase in Mung Bean Hypocotyl Plasma Membrane : Suggestion for A New Type of Higher Plant Plasma Membrane ATPase
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概要
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A vanadate-sensitive and nitrate-resistant ATPase was solubilized with Zwittergent 3-14 from a highly purified plasma membrane fraction of mung bean hypocotyls and partially purified by glycerol density gradient centrifugation and phenyl-Sepharose column chromatography. Either phosphatidylcholine or phosphatidylserine in addition to Mg^<2+> was required for the enzyme activity, whereas K^+ , phosphatidylethanolamine and lysophosphatidylcholine had no effect on the activity. The purified enzyme preparation contained two major polypeptides with molecular masses of 67 and 55 kDa as analyzed by SDS-polyacrylamide gel electrophoresis. When the plasma membrane fraction was incubated with [γ-^<32>P]ATP, a 45-70-kDa polypeptide(s) was labeled, and the label could be rapidly chased with cold ATP. When the fraction was incubated with [^<14>C]N,N'-dicyclohexylcarbodiimide, an inhibitor for the ATPase, a 15-20-kDa polypeptide was labeled. We propose that the enzyme is a new type of higher plant plasma membrane ATPase and is composed of 67- and 55-kDa subunits and probably also a 15-20-kDa subunit.
- 日本植物生理学会の論文
著者
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Asahi Tadashi
Laboratory of Biochemistry, School of Agriculture, Nagoya University
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Kimura T
Nagoya Univ. Nagoya Jpn
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Kimura Tetsuya
Laboratory of Applied Microbiology, Faculty of Bioresources, Mie University
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Asahi Tadashi
Laboratory Of Biochemistry School Of Agriculture Nagoya University
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Mito Nobuaki
Laboratory of Biochemistry, School of Agriculture, Nagoya University
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Mito Nobuaki
Laboratory Of Biochemistry School Of Agriculture Nagoya University:(present)takarazuka Institute Sum
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Asahi Tadashi
Laboralory Of Biochemistry Faculty Of Agriculture Nagoya University
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