Abstract
InCarcinus maenashaemolymph, zinc is almost entirely bound to the respiratory pigment, which is the copper-protein haemocyanin (Hc). Zinc ions are loosely bound, as indicated by the low value of the association constant (k= 1.7 × 105M-1at pH = 8.0). The number of binding sitesNis equal to 4 per minimal functional subunit (75000 Dalton). No co-operativity has been found between the different metal sites. Data reported in this paper support the hypothesis that haemocyanin can act as metal carrier in the haemolymph ofC. maenas.

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