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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 
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.

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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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