Conservation of electron transport and energy transfer reactions of spinach chloroplasts in glycero

When spinach chloroplasts were suspended in 50% glycerol inthe presence of 5 mM sodium chloride, then stored at –20°Cactivity of the Hill reaction was retained for several monthswith a small loss. Under these conditions photophosphorylationactivity was reduced by half during the month of storage. (Received February 2, 1971; )     

Purification and properties of cytochrome c and two peroxidases from spinach leaves

1. A simultaneous purification procedure of cytochrome c, peroxidases,ferredoxin, ferredoxin-NADP reductase and sulfite reductasefrom spinach leaves is described. Cytochrome c, ferredoxin andferredoxin-NADP reductase were prepared in crystalline states.The two peroxidases were obtained in homogeneous states as evidencedby their electrophoretic patterns on acrylamide gel and sedimentationanalysis. 2. Crystalline cytochrome c showed a molecular weight of 13,800and an E₀' of 270 mv at pH 7.0. In addition to these properties,its spectral pattern also indicated that this cytochrome c wasderived from mitochondria. 3. Two peroxidases were isolated in high spin forms after treatmentwith HgCl₂. They had a-peaks at 556 mµ in their reducedforms. Although both peroxidases showed small differences inchromatographic behavior on a carboxymethyl cellulose column,' they had similar spectral properties, dissociation constantsof peroxidase-cyanide complex and rate constants for peroxidasereactions. (Received December 24, 1970; )