[HTML][HTML] Hyperactive antifreeze protein from beetles

LA Graham, YC Liou, VK Walker, PL Davies - Nature, 1997 - nature.com
LA Graham, YC Liou, VK Walker, PL Davies
Nature, 1997nature.com
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. Figure 1 Thermal hysteresis activity of Tenebrio haemolymph as a function of …
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 .
Figure 1
Thermal hysteresis activity of Tenebrio haemolymph as a function of dilution.
The standard deviation of each sample (n43) is shown.
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