Advertisement

Characterization of Purified Cytochrome P-450scc and P-45011β from Bovine Adrenocortical Mitochondria

  • Masayuki Katagiri
  • Shigeki Takemori
  • Eiji Itagaki
  • Katsuko Suhara
  • Tomoharu Gomi
  • Hiroshi Sato
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 74)

Abstract

In the adrenal cortex, NADPH-adrenal ferredoxin reductase (adrenodoxin reductase)-adrenal ferredoxin (adrenodoxin)-cytochrome P-450 system has been known to be associated with the mitochondrial steroid hydroxylase activities, viz., cholesterol side-chain cleavage and steroid 11β- and 18-hydroxylations. In order to elucidate the reaction mechanism of the hydroxylase system, it is important that each component is available in a pure form. As previously reported, adrenodoxin reductase (1) and adrenodoxin (2,3) have been obtained in a pure state. The latter has been crystallized. Details will be discussed in a separate chapter (4).

Keywords

Sodium Cholate Mitochondrial Pellet Performic Acid Electron Transfer System Sedimentation Velocity Experiment 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Suhara, K., Ikeda, Y., Takemori, S., and Katagiri, M., Fed. Eur. Biochem. Soc. Lett., 28, 45 (1972).CrossRefGoogle Scholar
  2. 2.
    Suhara, K., Takemori, S., and Katagiri, M., Biochim. Biophys. Acta, 263, 272 (1972).PubMedCrossRefGoogle Scholar
  3. 3.
    Suhara, K., Kanayama, K., Takemori, S., and Katagiri, M., Biochim. Biophys. Acta, 336, 309 (1974).CrossRefGoogle Scholar
  4. 4.
    Takemori, S., Suhara, K., and Katagiri, M., This book, p.36Google Scholar
  5. 5.
    Hashimoto, S., Suhara, K., Takemori, S., and Katagiri, M., Seikagaku, 43, 535 (1971).Google Scholar
  6. 6.
    Katagiri, M., and Takemori, S., Abstract Book, Ninth International Congress of Biochemistry, Stockholm, p. 327 (1973).Google Scholar
  7. 7.
    Takemori, S., Suhara, K., Hashimoto, S., Hashimoto, M., Sato, H., Gomi, T., and Katagiri, M., Biochem. Biophys. Res. Commun., 63, 588 (1975).PubMedCrossRefGoogle Scholar
  8. 8.
    Takemori, S., Sato, H., Gomi, T., Suhara, K., and Katagiri, M., Biochem. Biophys. Res. Commun., 67, 1151 (1975).PubMedCrossRefGoogle Scholar
  9. 9.
    Omura, T., Sanders, E., Estabrook, R. W., Cooper, D. Y., and Rosenthal, O., Arch. Biochem. Biophys., 117, 660 (1966).CrossRefGoogle Scholar
  10. 10.
    Ando, N., and Horie, S., J. Biochem., 65, 269 (1969).Google Scholar
  11. 11.
    Mattingly, D., J. Clin. Pathol., 15, 374 (1962).PubMedCrossRefGoogle Scholar
  12. 12.
    Björkhem, I., and Karlmar, K-E., Eur. J. Biochem., 51, 145 (1975).PubMedCrossRefGoogle Scholar
  13. 13.
    Hirs, C. H. W., J. Biol. Chem., 219, 611 (1956).PubMedGoogle Scholar
  14. 14.
    Goodwin, T. W., and Morton, R. A., Biochem. J., 40, 628 (1946).PubMedGoogle Scholar
  15. 15.
    Van de Bogart, M., and Beinert, H., Anal. Biochem., 20, 325 (1967).PubMedCrossRefGoogle Scholar
  16. 16.
    Ballou, D. R., Veeger, C., Van der Hoeven, T. A., and Coon, M. J., Fed. Eur. Biochem. Soc. Lett., 38, 337 (1974).CrossRefGoogle Scholar
  17. 17.
    Appleby, C. A., and Morton, R. K., Biochem. J., 73, 539 (1959).PubMedGoogle Scholar

Copyright information

© Plenum Press, New York 1976

Authors and Affiliations

  • Masayuki Katagiri
    • 1
  • Shigeki Takemori
    • 1
  • Eiji Itagaki
    • 1
  • Katsuko Suhara
    • 1
  • Tomoharu Gomi
    • 1
  • Hiroshi Sato
    • 1
  1. 1.Department of Chemistry, Faculty of ScienceKanazawa UniversityIshikawa 920Japan

Personalised recommendations