Abstract
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.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
