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Metallothionein and Metallothionein-Like Proteins: Physiological Importance

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Advances in Comparative and Environmental Physiology

Part of the book series: Advances in Comparative and Environmental Physiology ((COMPARATIVE,volume 5))

Abstract

Since the initial demonstration of a low-molecular weight cadmium-binding protein in mammals, the research on the function of these proteins, which also can bind Cu, Zn, and Hg, has been focused primarily on their detoxifying properties. Such a direction is understandable, since the synthesis of the proteins can be induced by these potentially toxic metal ions. These proteins, isolated from mammals, have structural characteristics that are very different from those of most proteins, such as having 30% of the amino acid residues as cysteine and having the capacity to bind 7 mol of cadmium, zinc, or mercury or 12 mol copper per mole of protein. The binding of metal to these proteins is through thiol bonding, and therefore, the name metallothionein was proposed and accepted (throughout the text metallothionein will be denoted as MT).

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Authors and Affiliations

  1. National Marine Fisheries Service, Southeast Fisheries Center, Beaufort Laboratory, NOAA, Beaufort, North Carolina, 28516, USA

    David W. Engel

  2. Marine Biomedical Center, Duke University Marine Laboratory, Beaufort, North Carolina, 28516, USA

    Marius Brouwer

Authors
  1. David W. Engel
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  2. Marius Brouwer
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© 1989 Springer-Verlag Berlin Heidelberg

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Engel, D.W., Brouwer, M. (1989). Metallothionein and Metallothionein-Like Proteins: Physiological Importance. In: Advances in Comparative and Environmental Physiology. Advances in Comparative and Environmental Physiology, vol 5. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-74510-2_3

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  • DOI: https://doi.org/10.1007/978-3-642-74510-2_3

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-74512-6

  • Online ISBN: 978-3-642-74510-2

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