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Inhibition of Lectins by Antifreeze Glycoproteins from an Antarctic Fish

Nature volume 242, pages 342–343 (1973)Cite this article

Abstract

CERTAIN Antarctic fishes can resist freezing, even at ambient water temperatures as low as −1.9° C, partly because of the presence in their serum of a unique group of “antifreeze” glycoproteins1–5. These glycoproteins are composed of repeating units of the triglycopeptide, Ala-Ala-Thr-O-disaccharide. The disaccharide is galactosyl-N-acetylgalactosamine, with internal linkage β, 1→3 (ref. 6) or (β, 1→4 (ref. 7). Three active glyco-proteins differing only in polymer length have been characterized with molecular weights of approximately 11,000, 17,000, and 22,000. In addition to these active glycoproteins, two smaller related glycoproteins have been found. These differ from the large active glycoproteins by their comparative inactivity in depressing the freezing point, their smaller molecular weights (approximately 2,500 and 4,500), and the substitution of a proline for some of the alanines following threonine8,9.

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Authors and Affiliations

  1. Immunohematology Laboratory, Department of Pathology, New York University School of Medicine, New York, 10016

    JOSEPH V. CHUBA & WILLIAM J. KUHNS

  2. Osborn Laboratories of Marine Sciences, New York Zoological Society, New York Aquarium, Brooklyn, New York, 11224

    Ross F. NIGRELLI

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

    JACKIE R. VANDENHEEDE, DAVID T. OSUGA & ROBERT E. FEENEY

Authors
  1. JOSEPH V. CHUBA
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  2. WILLIAM J. KUHNS
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  3. Ross F. NIGRELLI
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  4. JACKIE R. VANDENHEEDE
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  5. DAVID T. OSUGA
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  6. ROBERT E. FEENEY
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CHUBA, J., KUHNS, W., NIGRELLI, R. et al. Inhibition of Lectins by Antifreeze Glycoproteins from an Antarctic Fish. Nature 242, 342–343 (1973). https://doi.org/10.1038/242342a0

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