胡杨CBL1蛋白溶液的DSC研究  

A DSC Study of CBL1 Protein of Populus

作　　者：刘郑[1] 鲁芳[1] 冯舵[1] 张文杰[1] 高伟[1] 

机构地区：[1]北京林业大学理学院,北京100083

出　　处：《中国农学通报》2014年第22期28-34,共7页Chinese Agricultural Science Bulletin

基　　金：国家自然科学基金(30970578;31070651);教育部新世纪优秀人才支持计划资助项目(NECT-08-0731)

摘　　要：胡杨CBL1蛋白是一类重要的钙信号转导蛋白,在植物应对干旱、低温、高pH等环境胁迫中发挥着重要作用。通过差示扫描量热法,研究胡杨CBL1蛋白在-30~0℃与20~95℃的温度条件下的热力学性质。结果表明,虽然胡杨CBL1蛋白在应对低温环境胁迫中发挥作用,但是胡杨CBL1蛋白本身并不具有抗冻性能,且其熔化过程中的冰晶含量与保留温度呈指数对应关系;而在加热过程中,胡杨CBL1蛋白在81.6℃左右不可逆变性,在变性之前胡杨CBL1蛋白的熵与焓增量逐渐减小,在变性之后熵与焓迅速增加,显示出胡杨CBL1蛋白具有较高的热稳定性。The CBL1 protein is an important class of calcium signal proteins, which can response to drought, low temperature, high pH and other environmental stress. The differential scanning calorimetry was applied to study thermal properties of CBL1 protein of Populus although during-30℃ to 0℃ and 20℃ to 95℃. It was found that the CBL1 protein of Populus played a role in response to low temperature stress, itself did not have frost resistance, meanwhile in the melting process, the ice content and temperature had exponential relationship. During the heating process, the irreversible denaturation temperature of CBL1 protein was about 81.6℃, meanwhile the performance of the entropy and enthalpy decreased in increments when it was below the denaturation temperature once reaching the denaturation temperature, the entropy and enthalpy increased rapidly, which showed a high thermal stability of CBL 1 protein of Populus.

关 键 词：胡杨CBL1蛋白 差示扫描量热法(DSC) 熵 焓 

分 类 号：Q6[生物学—生物物理学]