Partial saturation of rat liver Cd-binding proteins by Cd2+ in vivo

  • R. D. Irons
  • J. C. Smith
Article

Abstract

Liver Cd-binding proteins (Cd-BP) were isolated from rats chronically treated with109Cd-labeled CdCl2 for ten days. Fractions purified using Sephadex G-75 and DEAE-Sephadex were characterized and found to be similar to those isolated by other investigators. Cd-binding was not saturated in any of the preparations and significant amounts of Cu and Zn were also found bound to the proteins. The percentage of saturation for Cd-BP1, and Cd-BP2 was independently determined by atomic absorption spectrometry and spectroscopy at 254 nm. These results indicate that the fraction of binding sites unoccupied by Cd on Cd-BP approaches 20%in vivo.

Keywords

Spectroscopy CdCl2 Atomic Absorption Atomic Absorption Spectrometry Absorption Spectrometry 

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Copyright information

© Springer-Verlag New York Inc. 1977

Authors and Affiliations

  • R. D. Irons
    • 1
  • J. C. Smith
    • 2
  1. 1.Dept. of PathologyUniversity of Rochester School of Medicine & DentistryRochester
  2. 2.Dept. of PharmacologyUniversity of Rochester School of Medicine & DentistryRochester

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