Journal of Comparative Physiology B

, Volume 181, Issue 6, pp 713–719 | Cite as

Antifreeze proteins in the Antarctic springtail, Gressittacantha terranova

Original Paper

Abstract

Antarctic springtails are exemplars of extreme low temperature adaptation in terrestrial arthropods. This paper represents the first examination of such adaptation in the springtail, Gressittacantha terranova. Acclimatization state was measured in field-fresh samples over a 22-day period at the beginning of the austral summer. No evidence of temperature tracking was observed. Mean temperature of crystallization (T c) for all samples was −20.67 ± 0.32°C and the lowest T c recorded was −32.62°C. Ice affinity purification was used to collect antifreeze proteins (AFPs) from springtail homogenate. The purified ice fraction demonstrated both thermal hysteresis activity and recrystallisation inhibition. Growth-melt observations revealed that ice crystals grow normal to the c-axis (basal plane). Reverse-phased HPLC produce one clearly resolved peak (P1) and one compound peak (P2). Mass spectrometry identified the molecular mass of P1 as 8,599 Da. The P1 protein was also the most prominent in P2, although additional peptides of 6–7 KDa were also prominent. The main AFP of the Antarctic springtail, G. terranova has been isolated, although like other AFP-expressing arthropods, it shows evidence of expressing a family of AFPs.

Keywords

Antifreeze protein Antarctica Collembola Supercooling Thermal hysteresis 

Abbreviations

AFP

Antifreeze protein

HPLC

High performance liquid chromatography

RI

Recrystallisation inhibition

Tc

Temperature of crystallization

TH

Thermal hysteresis

Notes

Acknowledgments

TCH was funded by the Leverhulme Trust. Thanks to Antarctic NZ for logistical support.

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Copyright information

© Springer-Verlag 2011

Authors and Affiliations

  1. 1.Department of ZoologyUniversity of OtagoDunedinNew Zealand
  2. 2.Department of BiochemistryUniversity of OtagoDunedinNew Zealand

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