Purification and Characterization of Phosphoribulokinase from the Cyanobacterium Synechococcus PCC7942 : PROTEINS, ENZYMES AND METABOLISM
スポンサーリンク
概要
- 論文の詳細を見る
Phosphoribulokinase (PRK) was purified to electrophoretic homogeneity from Synechococcus PCC7942 with high specific activity. Molecular masses of the native enzyme and its subunit were 178 and 42 kDa, respectively. Cys-17 and Cys-38 were conserved in the cyanobacterial PRK, but 18 amino acid residues between them were missing among the 40 residues found in higher plant PRKs.
- 日本植物生理学会の論文
著者
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Iwaki Toshio
Department of Agricultural Chemistry, University of Osaka Prefecture
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Iwaki Toshio
Department Of Applied Biochemistry University Of Osaka Prefecture
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Wadano A
Dept.applied Biol.chem. Osaka Pref.univ.
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Wadano Akira
Department Of Agricultural Chemistry College Of Agriculture University Of Osaka Prefecture
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Kamata Yoichi
Department of Veterinary Medicine, University of Osaka Prefecture
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Nishikawa Keisuke
Department of Applied Biochemistry, University of Osaka Prefecture
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Hirahashi Tomohiro
Department of Applied Biochemistry, University of Osaka Prefecture
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Hirahashi Tomohiro
Dept. Applied Biol. Chem. Univ. Osaka. Pref.
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Nishikawa Kazuko
Dept. Applied Biol. Chem. Univ. Osaka. Pref.
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Kamata Yoichi
Department Of Veterinary Medicine University Of Osaka Prefecture
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