Thermodynamic study on conformation change of carbonic anhydrase
Thermodynamic study on conformation change of carbonic anhydrase作者机构：Chinese Acad Sci Inst Chem Beijing 100080 Peoples R China
出 版 物：《Chinese Science Bulletin》 (科学通报(英文版))
年 卷 期：1998年第43卷第21期
页 面：1802-1805页
核心收录：
学科分类：0710[理学-生物学] 071010[理学-生物化学与分子生物学] 07[理学]
基 金：ThisworkwassupportedbytheNationalNaturalScienceFoundationofChina (GrantNo .2 96 330 2 0 )
主 题：carbonic anhydrase conformation change DSC thermodynamics
摘 要：The effect of pHs on structural stability of the zinc-containing metalloenzyme carbonic anhydrase has been studied by means of differential scanning calorimetry. The rule of the conformational change for the enzyme with pH change has been found by thermodynamic analysis. The experimental results also provide valuable information: in the pH range from 5.26 to 9.04, two independent endothermal peaks were observed on DSC thermogram. It shows the existence of two structural domains in the molecule. The transition temperature and enthalpy of the two domains are different.
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