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1984•Journal of the Marine Biological Association of the United KingdomRequires access

Zinc transport in the haemolymph ofCarcinus maenas(Crustacea: Decapoda)

Paolo Zatta

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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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What this paper is about

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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Available 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.

Key concepts: Carcinus maenas, Hemolymph, Decapoda, Crustacean, Zinc, Hemocyanin, Biology, Copper

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