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Zinc transport in the haemolymph of Carcinus maenas (Crustacea: Decapoda)

Published online by Cambridge University Press:  11 May 2009

Paolo Zatta
Paolo Zatta
Affiliation:
C.N.R.-Centro di studio per la Fisiologia e la Biochimica delle Emocianine e di altre Metallo-Proteine, Via Loredan 10, 35131 Padova, Italy
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Abstract

In Carcinus maenas haemolymph, 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 × 105 M-1 at pH = 8.0). The number of binding sites N is 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 of C. maenas.

Type
Research Article
Information
Journal of the Marine Biological Association of the United Kingdom , Volume 64 , Issue 4 , November 1984 , pp. 801 - 807
Copyright
Copyright © Marine Biological Association of the United Kingdom 1984

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