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The nature of zinc and copper complexes in the oyster Ostrea edulis

Abstract

The zinc and copper associated with the soft tissues of the oyster Ostrea edulis Linnaeus have been separated into a soluble component and a tissue-residue, cell-debris bound component. In the case of zinc, the tissue-bound component was found to contain at least two species of complex; a firmly-bound species, exchangeable with 65Zn2+ and a less-firmly, reversibly-bound species, exchangeable with 65Zn2+. The soluble component, which constitutes some 40% of the total zinc and copper, was fractionated on Sephadex G-25 and the zinc and copper shown to be weakly-complexed to the small molecular weight compounds, taurine, lysine, ATP and possibly homarine (N-methyl-α-picolinic acid) and to be fully exchangeable with 65Zn2+. These soluble complexes can act as a freely available mobile reserve of metal to ensure a constant saturation of metal-dependent enzyme systems operating under adverse environments. Sephadex G-25 acts as a weak ion-exchange resin, which can cause a translocation of zinc and copper from its soluble weak complexes and result in the spurious association of the metals with other compounds.

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Communicated by J.H.S. Blaxter, Oban

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Coombs, T.L. The nature of zinc and copper complexes in the oyster Ostrea edulis . Marine Biology 28, 1–10 (1974). https://doi.org/10.1007/BF00389111

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Keywords

  • Copper
  • Zinc
  • Lysine
  • Taurine
  • Enzyme System