Purification and properties of cytochrome c and two peroxidases from spinach leaves
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概要
- 論文の詳細を見る
1. A simultaneous purification procedure of cytochrome c, peroxidases, ferredoxin, ferredoxin-NADP reductase and sulfite reductase from spinach leaves is described. Cytochrome c, ferredoxin and ferredoxin-NADP reductase were prepared in crystal-line states. The two peroxidases were obtained in homogeneous states as evidenced by their electrophoretic patterns on acrylamide gel and sedimentation analysis. 2. Crystalline cytochrome c showed a molecular weight of 1 3,800 and an E_o' of 270 mv at pH 7.0. In addition to these properties, its spectral pattern also indicated that this cytochrome c was derived from mitochondria. 3. Two peroxidases were isolated in high spin forms after treatment with HgCl_2. They had a-peaks at 556 mμ in their reduced forms. Although both peroxidases showed small differences in chromatographic behavior on a carboxymethyl cellose column, they had similar spectral properties, dissociation constants of peroxidase-cyanide complex and rate constants for peroxidase reactions.
- 日本植物生理学会の論文
著者
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Asada Kozi
The Research Institute For Food Science Kyoto University
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Takahashi Masa-aki
The Research Institute For Food Science Kyoto University
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Takahashi Masa-aki
The Research Institulefor Fbod Science Kyoto University
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Asada Kozi
The Research Institulefor Fbod Science Kyoto University
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