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Macromolecules from cold-adapted antarctic fishes

Naturwissenschaften volume 59, pages 22–29 (1972)Cite this article

Abstract

The article reviews the studies of the authors and other investigators on blood proteins and muscle and brain enzymes from Antarctic fishes adapted to the −1.85 °C temperature of the ice-salt water of McMurdo Sound, Antarctica. The bloods had two major characteristics related to the cold-adaptation: a rapid rate of clotting of the blood at 0 °C and a very specialized type of glycoprotein (antifreeze protein) responsible for the prevention of freezing of the blood. This antifreeze protein has the repeating structure of a glycotripeptide consisting of units of alanine, alanine, threonine with each threonine glycosidically linked to a disaccharide of galactosyl-N-acetyl galactosamine. Six enzymes studied were muscle fructose-1,6-diphosphate aldolase, glyceraldehyde-3-phosphate dehydrogenase, glycogen phosphorylase, and lactic dehydrogenase, heart mitochondrial cytochrome system, and brain tissue acetylcholinesterase. Adaptations for efficient catalysis at low temperatures included a low activation energy (for catalysis) and a resistance to inactivation at low temperature, but there was no general property characteristic of low temperature adaptation.

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Affiliations

  1. Department of Food Science and Technology, University of California, 95616, Davis, California, USA

    R. E. Feeney, J. Vandenheede & D. T. Osuga

Authors
  1. R. E. Feeney
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  2. J. Vandenheede
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  3. D. T. Osuga
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Additional information

The researches providing the background for this article were supported by the Office of Polar Programs of the U.S. National Science Foundation.

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Feeney, R.E., Vandenheede, J. & Osuga, D.T. Macromolecules from cold-adapted antarctic fishes. Naturwissenschaften 59, 22–29 (1972). https://doi.org/10.1007/BF00594619

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  • DOI: https://doi.org/10.1007/BF00594619

Keywords

  • Threonine
  • Diphosphate
  • Disaccharide
  • Acetylcholinesterase
  • Phosphorylase