Abstract
PARTIAL purification of a cytochrome component from Porphyra tenera, a component which has absorption peaks similar to that of cytochrome c or c 1 was first reported by Yakushiji1. Recently, Katoh and Takamiya (ref. 2 and Katoh, S., and Takamiya, A., personal communication) succeeded in obtaining a crystalline preparation of this component by means of diethylaminoethyl-cellulose column chromatography and reported the redox-potential of this and other components in marine algae. We also have crystallized the cytochrome by means of a cation-exchanger at pH 5.0. Since the diethylaminoethyl-cellulose column procedure is possible at pH 7.0, this procedure may be better; our method can be used to purify not only basic enzyme proteins, but also those that are stable in acidic pH.
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References
Yakushiji, E., Acta Phytochim., 8, 325 (1935).
Katoh, S., J. Biochem. (Japan), 46, 629 (1959).
Kohn, J., Nature, 183, 1055 (1959).
Horio, T., Higashi, T., Matsubara, H., Kusai, K., Nakai, M., and Okunuki, K., Biochim. Biophys. Acta, 29, 297 (1958).
Okunuki, K., Sekuzu, I., Yonetani, T., and Takemori, S., J. Biochem. (Japan), 45, 847 (1958).
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YAKUSHIJI, E., SUGIMURA, Y., SEKUZU, I. et al. Preparation of Crystalline Cytochrome553 from Porphyra tenera . Nature 185, 105–106 (1960). https://doi.org/10.1038/185105a0
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DOI: https://doi.org/10.1038/185105a0
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