Antifreeze glycoproteins from the antarctic fish Dissostichus mawsoni studied by differential scanning calorimetry (DSC) in combination with nanolitre osmometry.
This study investigates in detail the freezing events during cooling of solutions of various size classes of antifreeze glycoproteins. Differential scanning calorimetry and nanolitre osmometry were used to observe ice growth at temperatures within the hysteresis gap between the melting point and non-equilibrium freezing point (hysteresis freezing point) of solutions of the various sized antifreeze glycoproteins (AFGPs). The ice growth within the hysteresis gap is presumably due to both the expression of primary or near primary prism planes and also some growth at the basal plane. The binding of the AFGPs to the ice causes a particular ice crystal morphology. With the smaller AFGPs, substantial microscopic ice growth was observed in the form of a hexagonal bipyramids within the hysteresis gap.
Ramløv
Hans
H
Department of Biology and Chemistry, Roskilde University, Roskilde, Denmark. HR@ruc.dk
DeVries
Arthur L
AL
Wilson
Peter W
PW
D000818:Animals; D000864:Antarctic Regions; D021301:Antifreeze Proteins / Q000737:chemistry*; D002152:Calorimetry, Differential Scanning; D003460:Crystallization; D005399:Fishes; D007053:Ice; D009994:Osmolar Concentration; D044366:Transition Temperature
D021301:Antifreeze Proteins; D007053:Ice