Abstract
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 crystalline 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 13,800 and an E0′ 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 HgCl2. They had a-peaks at 556 mμ in their reduced forms. Although both peroxidases showed small differences in chromatographic behavior on a carboxymethyl cellulose column, ' they had similar spectral properties, dissociation constants of peroxidase-cyanide complex and rate constants for peroxidase reactions.
Keywords
FerredoxinPeroxidaseCytochrome c peroxidaseChemistrySpinachCytochrome cCytochromeReductaseSulfite reductaseStereochemistryChromatographyBiochemistryEnzymeMitochondrion
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- Year
- 1971
- Type
- article
- Citations
- 22
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Kozi Asada,
Masaaki Takahashi
(1971).
Purification and properties of cytochrome <italic>c</italic> and two peroxidases from spinach leaves.
Plant and Cell Physiology
.
https://doi.org/10.1093/oxfordjournals.pcp.a074630
Identifiers
- DOI
- 10.1093/oxfordjournals.pcp.a074630