Purification of H^+-ATPase from the Plasma Membrane of Maize Roots and Preparation of Its Antibody
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概要
- 論文の詳細を見る
The plasma membrane ATPase was purified to near homogeneity from corn roots. Procedures included partition in an aqueous polymer two-phase system, solubilization of the enzyme from plasma membranes with lysolecithin, and vertical centrifugation with a glycerol gradient. The purified enzyme had a high specific activity [4.7 μmol・min^<-1>・(mg protein)^<-1>] absolutely requiring potassium ions for catalytic function. A specific polyclonal antibody was produced against the 90-kDa polypeptide of the enzyme.
- 日本植物生理学会の論文
著者
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Nagao Toshihiro
Department Of Agricultural Chemistry School Of Agriculture Nagoya University
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Sugiyama Tatsuo
Department Of Agricultural Chemistry School Of Agriculture Nagoya University
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Sugiyama Tatsuo
Department Of Agricultural Chemistry Faculty Of Agriculture Nagoya University
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Sadakawa Hideo
Department of Agricultural Chemistry, School of Agriculture, Nagoya University
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Sadakawa Hideo
Department Of Agricultural Chemistry School Of Agriculture Nagoya University
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