|
生物物理学报 1995
DIRECT MEASUREMENT OF THERMAL HYSTERESIS EFFECT OF ANTINFREEZE PROTEIN SOLUTION BY DIFFERENTIAL SCANNING CALORIMETRY
|
Abstract:
The direct micrescopic observation has been used to measure the thermal hysteresis effects of antifreeze proteins in the litelature. The amount of ice Crystals in the system is roughly estimated by the obserVed volume of ice nudei, and thus it is much more artffidal. Here we report a dired differential scanning calorimetric measUrement of the thermal hysteresis effete of antifreeze protein sulution from arnmopiptanthus mongolicus. The thennal hystersis temperature and amount of ice crystal nuclei are quantitatively measured from DSC thennograms, melting and freezing enthalpies. Compared to the results reported in the literature, this antifreeze protein shows 2 much higher antifreeze activity and thus a new and accurate proedure to measure the aCtivity of antitreeze protein solution is provided.