A nonprotein thermal hysteresis-producing xylomannan antifreeze in the freeze-tolerant Alaskan beetle Upis ceramboides.

Proceedings of the National Academy of Sciences of the United States of America
Kent WaltersJohn G Duman

Abstract

Thermal hysteresis (TH), a difference between the melting and freezing points of a solution that is indicative of the presence of large-molecular-mass antifreezes (e.g., antifreeze proteins), has been described in animals, plants, bacteria, and fungi. Although all previously described TH-producing biomolecules are proteins, most thermal hysteresis factors (THFs) have not yet been structurally characterized, and none have been characterized from a freeze-tolerant animal. We isolated a highly active THF from the freeze-tolerant beetle, Upis ceramboides, by means of ice affinity. Amino acid chromatographic analysis, polyacrylamide gel electrophoresis, UV-Vis spectrophotometry, and NMR spectroscopy indicated that the THF contained little or no protein, yet it produced 3.7 +/- 0.3 degrees C of TH at 5 mg/ml, comparable to that of the most active insect antifreeze proteins. Compositional and structural analyses indicated that this antifreeze contains a beta-mannopyranosyl-(1-->4) beta-xylopyranose backbone and a fatty acid component, although the lipid may not be covalently linked to the saccharide. Consistent with the proposed structure, treatment with endo-beta-(1-->4)xylanase ablated TH activity. This xylomannan is the first TH-pr...Continue Reading

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Citations

Feb 1, 2011·Journal of Comparative Physiology. B, Biochemical, Systemic, and Environmental Physiology·Kent R WaltersJohn G Duman
Mar 15, 2011·Journal of Comparative Physiology. B, Biochemical, Systemic, and Environmental Physiology·T C HawesD A Wharton
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