Skip to main content

Implication of Ligand Modified Spectra of Cytochrome P-450 Associated with Pregnenolone Synthesis in Mitochondria from Corpus Luteum

  • Chapter
Cytochromes P-450 and b5

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 58))

Abstract

It is now well established that many reagents can modify the cytochrome P-450 spectrum. These modifications are produced. by the interaction of ligands with hemoprotein or the iron of the heme prosthetic group (13). The modified cytochrome P-450 difference spectra have been classified as Type I if the induced maximum in the Soret region is at 390 nm and the minimum at 420 nm, as reverse Type I if the positions of the maximum and minimum are reversed, and as Type II if the maximum and minimum are reversed and both shifted by 5 to 10 nm to the red end of the spectrum (12).

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 39.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 54.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Burstein, S., Co, N., Gut, M., Schleyer, H., Cooper, D. Y. and Rosenthal, O. 1972. Substrate-induced difference spectra and cholesterol to pregnenolone conversion with adrenal heme protein P-450. Biochemistry 11: 573–577.

    CAS  Google Scholar 

  2. Harding, B. W., Whysner, J. A., Cheng, S. C. and Ramseyer, J. 1970. Substrate induced changes in adrenal cortical cytochrome P-450, pp. 294–301. Hormonal Steroids, Excerpta Medica Int. Congr. Series #219, Proc. Illrd. Int. Congr., Hamburg, Sept. 1970.

    Google Scholar 

  3. Hochberg, R. B., van der Hoeven, T. A., Welch, M. and Lieberman, S. 1974. A simple and precise assay of the enzymatic conversion of cholesterol into pregnenolone. Biochemistry 13: 603–609.

    Article  PubMed  CAS  Google Scholar 

  4. Ichii, S., Omata, S., Kobayashi, S. 1967. Purification and some properties of cholesterol 20α-hydroxylase from hog adrenal mitochondria. Biochim. Biophys. Acta. 139:308–318.

    PubMed  CAS  Google Scholar 

  5. Luttrell, B., Hochberg, R. B., Dikon, W. R., McDonald, P.D. and Lieberman, S. 1972. Studies on the biosynthetic conversion of cholesterol into pregnenolone. J. Biol. Chem. 247:1462–1472.

    PubMed  CAS  Google Scholar 

  6. Mcintosh, E. N., and Salhanick, H. A. 1969. The effect of steroid hydroxylase inhibition on the rate of reduction of adrenal mitochondrial cytochrome P-450. Biochem. Biophys. Res. Commun. 37:552–558.

    Article  Google Scholar 

  7. Mcintosh, E. N., Mitani, F., Uzgiris, V. I., Alonso, C. and Salhanick, H. A. 1973. Comparative studies on mitochondrial and partially purified bovine corpus luteum cytochrome P-450. Ann. N.Y. Acad. Sci. 212:392–405.

    Article  PubMed  CAS  Google Scholar 

  8. Neville, A.M., and Engel, L.L. 1968. Inhibition of steroid A-isomerase of the bovine adrenal gland by substrate analogues. Endocrinology 83:873–876.

    Article  PubMed  CAS  Google Scholar 

  9. Mitani, F. and Horie, S. 1969. Studies on P-450. V. On the substrate-induced spectral change of P-450 solubilized from bovine adrenocortical mitochondria. J. Biochem. 65:269–280.

    PubMed  CAS  Google Scholar 

  10. Orrenius, S., Wilson, B.J., von Bahr, C. and Schenkman, J.B. 1972. On the significance of drug-induced spectral changes in liver microsomes, pp. 55–77. In G.S. Boyd and R.M.S. Smellie (ed.). Biological Hydroxylation Mechanisms. Academic Press, N.Y.

    Google Scholar 

  11. Raygatt, P.R. and Whitehouse, M.W. 1966. Substrates and in-hibitor specificity of the cholesterol oxidase in bovine adrenal cortex. Biochem. J. 101, S19:819–830.

    Google Scholar 

  12. Schenkman, J.B., Cinti, D.L., Orrenius, S., Moldeus, P. and Kraschnitz, R. 1972. The nature of the reverse Type I (modified Type II) spectral change in liver microsomes. Biochemistry 11:4243–4250.

    Article  PubMed  CAS  Google Scholar 

  13. Schleyer, H., Cooper, D.Y., Levin, S.S. and Rosenthal, O. 1972. Heme protein P-450 from the adrenal cortex: interaction with steroids and the hydroxylation reaction, pp. 187–206. In G.S. Boyd and R.M.S. Smellie (ed.). Biological Hydroxylation Mechanisms. Academic Press, N.Y.

    Google Scholar 

  14. Smith, A.L. 1967. Preparation, properties and conditions for assay of mitochondria: slaughter-house material, small scale. Methods Enzymol. 10:81–86.

    Article  CAS  Google Scholar 

  15. Sutherland, E.W., Cori, C.F., Haynes, R. and Olsen, N.S. 1949. Purification of the hyperglycemic-glycogenolytic factor from insulin and from gastric mucosa. J. Biol. Chem. 180: 825–837.

    PubMed  CAS  Google Scholar 

  16. Szarkowska, L. and Klingenberg, M. 1963. On the role of ubi-quinone in mitochondria. Biochem. Z. 338:674–697.

    PubMed  CAS  Google Scholar 

  17. Tsai, R., Yu, C.A., Gunsalus, I.C., Peisach, J., Blumberg, W., Orme-Johnson, W.H. and Beinert, H. 1970. Spin-state changes in cytochrome P-450cam on binding of specific substrates. Proc. Nat. Acad. Sci. 66:1157–1163.

    Article  PubMed  CAS  Google Scholar 

  18. Uzgiris, V.I., Mcintosh, E.N., Alonso, C. and Salhanick, H.A. 1971. Role of reversed electron transport in bovine corpus luteum mitochondrial steroid synthesis. Biochemistry 10: 2916–2923.

    Article  PubMed  CAS  Google Scholar 

  19. Yonetani, T. 1960. Studies on cytochrome oxidase. I. Abso-lute and difference absorption spectra. J. Biol. Chem. 235:845–852.

    PubMed  CAS  Google Scholar 

  20. Yonetani, T. and Ray, G.S. 1965. Studies on cytochrome oxi-dase. VI. Kinetics of the aerobic oxidation of ferrocyto-chrome c by cytochrome oxidase. J. Biol. Chem. 240:3392–3398.

    PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1975 Plenum Press, New York

About this chapter

Cite this chapter

Uzgiris, V.I., McIntosh, E.N., Graves, P., Salhanick, H.A. (1975). Implication of Ligand Modified Spectra of Cytochrome P-450 Associated with Pregnenolone Synthesis in Mitochondria from Corpus Luteum. In: Cooper, D.Y., Rosenthal, O., Snyder, R., Witmer, C. (eds) Cytochromes P-450 and b5 . Advances in Experimental Medicine and Biology, vol 58. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-9026-2_15

Download citation

  • DOI: https://doi.org/10.1007/978-1-4615-9026-2_15

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4615-9028-6

  • Online ISBN: 978-1-4615-9026-2

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics