Calorimetric analysis of antifreeze glycoproteins of the polar fish, Dissostichus mawsoni

Thomas N. Hansen, Arthur L. DeVries, John G. Baust

Research output: Contribution to journalArticlepeer-review


Solutions of antifreeze glycoproteins 1 through 5 and 8 were analyzed for activity by differential scanning calorimetry. With a scan rate of 1°C min-1, antifreeze glycoproteins 1-5 (20 mg/ml) revealed antifreeze activity with a delay in the freeze exotherm during cooling in the presence of ice. Antifreeze glycoprotein 8 (60 mg/ml), however, did not reveal antifreeze activity. When a 0.1°C min-1 scan rate was used, glycoproteins 1-5 again yielded a delay in the freeze onset, but the exotherm consisted of multiple events. At the slower scan glycoprotein 8 revealed an initial freeze followed by multiple exothermic events resembling those of glycoproteins 1-5. Thermograms exhibiting antifreeze activity had an initial shoulder in the exotherm direction upon cooling followed by a delay before the exotherm. The shoulders were correlated with c-axis ice growth observed in visual methods. The glycoprotein antifreezes had a linear increase in activity with decreased ice content.

Original languageEnglish (US)
Pages (from-to)169-173
Number of pages5
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Issue number2
StatePublished - Aug 30 1991


  • AFGP
  • Antarctic fish
  • DSC
  • Thermal hysteresis

ASJC Scopus subject areas

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Molecular Biology


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