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Hyperactive antifreeze protein from beetles

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Abstract

We have purified a thermal hysteresis (antifreeze) protein, with up to 100 times the specific activity of fish antifreeze proteins, from the common yellow mealworm beetle, Tenebrio molitor. It is a threonine- and cysteine-rich protein, of relative molecular mass 8,400, composed largely of 12-amino-acid repeats. We estimate that a concentration of roughly 1 mg ml−1 of this protein can account for the 5.5 °C of thermal hysteresis found in Tenebrio larvae (Fig. 1).

The standard deviation of each sample (n43) is shown.

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Figure 2: Predicted amino-acid sequences of four THP variants obtained from a fat-body cDNA library.
Figure 3: Photomicrographs of ice crystals grown in the presence of THP or AFP.

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Authors and Affiliations

  1. Departments of Biochemistry and Biology, Queens University, Kingston, K7L 1N6, Ontario, Canada

    Laurie A. Graham, Yih-Cherng Liou, Virginia K. Walker & Peter L. Davies

Authors
  1. Laurie A. Graham
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  2. Yih-Cherng Liou
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  3. Virginia K. Walker
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  4. Peter L. Davies
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Graham, L., Liou, YC., Walker, V. et al. Hyperactive antifreeze protein from beetles. Nature 388, 727–728 (1997). https://doi.org/10.1038/41908

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