Skip to main content
SpringerLink
Log in

The binding of various mercurial compounds to serum proteins

  • Published:
Bulletin of Environmental Contamination and Toxicology Aims and scope Submit manuscript

Summary

Binding study of Hg-labeled Hg2+, PMA, MMC and EMC to serum albumin of six mammalian species, bovine hemoglobin and bovine γglobulin is presented. Both MMC and EMC bound only weakly to serum albumin and γ-globulin and more strongly to hemoglobin; Hg2+ bound very strongly to both albumin and hemoglobin and weakly to γ-globulin; and PMA bound most strongly to albumin, next to hemoglobin and the least, to γ-globulin. The available binding sites varied from one to five per molecule of protein. Human serum albumin has the lowest association constants with all four mercurial compounds, indicating that it was not as tightly bound to mercurial compounds as found with serum albumins from other species.

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

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  • BARLTROP, D. and SMITH, A.M.: Experientia29, 1178 (1973).

    PubMed  Google Scholar 

  • CASTERLINE, J.L., Jr. and WILLIAM, C.H.: Bull. Environ. Cont. Tox.7, 292 (1971).

    Google Scholar 

  • ELLIS, R.W. and FANG, S.C.: Toxic. Appl. Pharmacol.20, 14 (1971).

    PubMed  Google Scholar 

  • FANG, S.C. The in vivo kinetics of mercury binding of kidney soluble proteins from rats receiving various mercurials. In: “Mercury, Mercurials, and Mercaptans.” M.M. Miller and T.W. Clarkson (editors). Charles C. Thomas Publisher, Springfield, Illinois, 1973, p. 277.

    Google Scholar 

  • INGRAM, V.M.: Biochem. J.59, 653 (1955).

    PubMed  Google Scholar 

  • KATZ, S.A. and WEISGERBER, H.E.: Experientia25, 672 (1969).

    PubMed  Google Scholar 

  • KATZ, S.A. and SAMITZ, M.H.: Environ. Res.6, 479 (1973).

    PubMed  Google Scholar 

  • NORSETH, T. and CLARKSON, T.W.: Arch. Environ. Hlth.21, 717 (1970).

    Google Scholar 

  • PERKIN, D.J.: Biochem. J.80, 668 (1961).

    PubMed  Google Scholar 

  • PROCKOP, D.J. and EBERT, P.S.: Anal. Biochem.6, 263 (1963).

    Google Scholar 

  • RAO, A.V., FALLIN, E. and FANG, S.C.: Plant Physiol.41, 443 (1966).

    PubMed  Google Scholar 

  • SCATCHARD, G.: Ann. N.Y. Acad. Sci.51, 660 (1949).

    Google Scholar 

  • TAKEDA, Y., KUNUGI, T., HOSHINO, O. and UKITA, T.: Toxicol. Appl. Pharmacol.13, 156 (1968).

    PubMed  Google Scholar 

  • ULFVARSON, U.: Int. Arch. Gewerbepath. Gewerbehygiene19, 412 (1962).

    Google Scholar 

  • WEBB, J.L.: Enzyme and metabolic inhibitors. Vol. II, Academic Press, New York, 1966, pp. 760.

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Agricultural Chemistry, Oregon State University, 97331, Corvallis, Oregon

    S. C. Fang & Elizabeth Fallin

Authors
  1. S. C. Fang
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Elizabeth Fallin
    View author publications

    You can also search for this author in PubMed Google Scholar

Additional information

Technical Paper No. 3982, Oregon Agricultural Experiment Station, Corvallis, Oregon. This investigation was supported in part by grant ES 00040-11 from the Institute of Environmental Science, U.S. Public Health Service.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Fang, S.C., Fallin, E. The binding of various mercurial compounds to serum proteins. Bull. Environ. Contam. Toxicol. 15, 110–117 (1976). https://doi.org/10.1007/BF01686202

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF01686202

Keywords

Search

Navigation