THERMAL HYSTERESIS ACTIVITY OF ANTIFREEZE PROTEIN SOLUTION A DIRECT DIFFERENTIAL SCANNING CALORIMETRIC MEASUREMENT
差示扫描量热法直接测定沙冬青抗冻蛋白的热滞效应

In this paper, we report a direct differential scanning calorimetic measurement of the low tempetature behavior of an antifreeze protein derived from Ammopiptanthus mongolicus The thermal hysteasis of this AFP is much more complicated than those of AFPs reports in the literature. Two exothermic or endothermic peaks at the low and high temperature sides were observed While the AFP solution was cooled or heatal. The tWO DSC peaks exhibit thermal hysteresis activity and are intertelated and interdependent. The antifreeze activity showed by the low temperature peak is higher than that by the high temperature peak. We suggest that the protein moled of this AFP may have two different kinds of interactions with and effects on water and ice crystal.