Uninduced Cu-Metallothionein and Other Cu-Binding Proteins in Mammals and Fish

  • D. H. Petering
  • S. Krezoski
  • T. Hartmann
  • Pu Chen
  • P. Onana
  • C. F. ShawIII

Abstract

Among species of metallothionein (Mt), the least understood are those containing copper. Relatively few reports on native Cu-Mt, isolated from organisms not exposed to Cu. Furthermore, there has been marked variability in reported Cu to protein stoichiometry and in the coordination number for sulfhydryl groups bound to Cu1–3. Hence, the experiments reported here focus on basic inorganic properties of a Cu,Zn-Mt isolated from bovine calf liver and survey fresh water fishes for the presence and characteristics of Cu,Zn-binding proteins (BP), analogous to Mt.

Keywords

Cytosol Sulfhydryl Penicillamine Nitrobenzoate Bathocuproine 

References

  1. 1.
    K. Lerch, Chemistry and Biology of Copper Metallothioneins, in Metal Ions in Biological Systems, 13, H. Siegel, ed., Marcel Dekker, New York, 1981.Google Scholar
  2. 2.
    I. Bremner, Involvement of metallothionein in the hepatic metabolism of copper. J. Nutr., 117: 19 (1986).Google Scholar
  3. 3.
    J. H. Freedman, L. Powers, and J. Peisach, Structure of the copper cluster in canine hepatic metallothionein using x-ray absorption spectroscopy. Biochem., 25: 2342 (1986).CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1988

Authors and Affiliations

  • D. H. Petering
    • 1
  • S. Krezoski
    • 1
  • T. Hartmann
    • 1
  • Pu Chen
    • 1
  • P. Onana
    • 1
  • C. F. ShawIII
    • 1
  1. 1.Department of ChemistryUniversity of Wisconsin-MilwaukeeMilwaukeeUSA

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