Abstract
A method has been described for the isolation and purification of two basic hemo-proteins, cytochrome c and peroxidase 556, from 70kg of rice embryo. The hemoproteins were extracted with dilute phosphate solution without any pretreatment with organic solvent. Ion exchange chromatography on CM-Sephadex C-50 and gel filtration chromato-graphy on Sephadex G-75 and G-100 were successfully applied for the purification. Both hemoproteins as major constituents were crystallized from ammonium sulfate solution, and some other chromoproteins, a blue protein and a flavoprotein, were also purified. Crystalline cytochrome c of rice embryo was found to be quite similar to cytochrome c of mammalian sources. Peroxidase 556 was found to spectroscopically belong to high spin form of peroxidases such as horseradish peroxidase II and Japanese-radish peroxidase a but it was a basic protein unlike to the latter two. Physiological significance of these hemoproteins is briefly discussed.
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