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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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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DOI: https://doi.org/10.1038/41908
