Hyperactive antifreeze protein from beetles

Laurie A. Graham, Yih-Cherng Liou, Virginia K. Walker and Peter L. Davies
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Laurie A. Graham: Queens University
Yih-Cherng Liou: Queens University
Virginia K. Walker: Queens University
Peter L. Davies: Queens University

Nature, 1997, vol. 388, issue 6644, 727-728

Abstract: 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). Figure 1 Thermal hysteresis activity of Tenebrio haemolymph as a function of dilution. The standard deviation of each sample (n43) is shown.

Date: 1997
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DOI: 10.1038/41908

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