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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