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Molluscan Hemocyanins: Structure and Function

  • Chapter
Blood and Tissue Oxygen Carriers

Part of the book series: Advances in Comparative and Environmental Physiology ((COMPARATIVE,volume 13))

Abstract

Hemocyanins are copper proteins that serve oxygen transport in two, and only two, phyla: Arthopoda and Mollusca. Although molluscan and arthropod hemocyanins share certain general features (for example, each has a binuclear copper site for oxygen binding) and exhibit much similarity in function, it is now becoming apparent that the structural differences between the hemocyanins from these two phyla are much more significant than their similarities. For example, size and arrangements of subunits are wholly different, and comparison of amino acid sequences indicates little homology except in one limited region. It is now generally held by workers in the field that the molluscan and arthropod hemocyanins are at best very distantly related, and probably arose in their separate phyla through independent evolutionary events (Mangum 1985; Drexel et al. 1987).

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  1. W. H. Lang

    Present address: Hutchinson Cancer Research Center, 1124 Columbia Street, Seattle, WA, 98104, USA

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  1. Department of Biochemistry and Biophysics, Oregon State University Corvallis, OR, 97331-6503, USA

    K. E. van Holde, K. I. Miller & W. H. Lang

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  1. K. E. van Holde
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  2. K. I. Miller
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  1. Department of Biology, The College of William and Mary, Williamsburg, Virginia, 23185, USA

    Charlotte P. Mangum

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van Holde, K.E., Miller, K.I., Lang, W.H. (1992). Molluscan Hemocyanins: Structure and Function. In: Mangum, C.P. (eds) Blood and Tissue Oxygen Carriers. Advances in Comparative and Environmental Physiology, vol 13. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-76418-9_10

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