Transfer of copper and zinc from ionic and metallothionein-bound forms to Cu, Zn--superoxide dismutase

Res Commun Mol Pathol Pharmacol. 1995 Mar;87(3):287-96.

Abstract

Reactivity in transfer of copper (Cu) and zinc (Zn) to their binding sites of superoxide dismutase (SOD) was examined in vitro by the HPLC/atomic absorption spectrophotometry. Ionic Cu (cuprous and cupric ions) were incorporated more efficiently than the metal bound to metallothionein. Cu binds not only to the Cu-binding site but also to the Zn-binding site. Although Zn in the reaction medium and the metal bound to the Zn-binding site of SOD affected little the reactivity in binding of ionic Cu, they disturbed the reactivity of Cu bound to metallothionein to the Cu-binding site. Both ionic and metallothionein-bound Zn were transferred at a comparable efficiency to the Zn-binding site but not to the Cu-binding site. Co-existing ionic Cu but not metallothionein-bound Cu in the medium inhibited the binding of Zn to SOD. The results indicate that ionic Cu can be transferred to both Cu- and Zn-binding sites of SOD more efficiently than metallothionein-bound Cu, while both ionic and metallothionein-bound Zn are transferred only to Zn-binding site at a comparable efficiency.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Binding Sites
  • Chromatography, High Pressure Liquid
  • Copper / metabolism*
  • Ions
  • Metallothionein / metabolism*
  • Rats
  • Rats, Inbred Strains
  • Spectrophotometry, Atomic
  • Superoxide Dismutase / metabolism*
  • Zinc / metabolism*

Substances

  • Ions
  • Copper
  • Metallothionein
  • Superoxide Dismutase
  • Zinc