Structural and functional changes of bovine carbonic anhydrase as a consequence of temperature.

N S Sarraf; A A Saboury; B Ranjbar; A A Moosavi-Movahedi

doi:10.18388/abp.2004_3551

Structural and functional changes of bovine carbonic anhydrase as a consequence of temperature.

N S Sarraf Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran.;
A A Saboury
B Ranjbar
A A Moosavi-Movahedi

DOI: https://doi.org/10.18388/abp.2004_3551

Abstract

The temperature dependence of the activity and structure of the enzyme carbonic anhydrase was studied. The Arrhenius plot shows a jump which is seen usually in proteins with more than one subunit or with one subunit but more than one domain. Since carbonic anhydrase has only one subunit with one domain, the fine conformational changes of the protein motifs could only be detected through circular dichroism polarimetry. It seems that the jump in Arrhenius plot is a result of some slight structural changes in the secondary and tertiary structures of the enzyme.

Published

2004-09-30

Issue

Vol. 51 No. 3 (2004)

Section

Articles

Acta Biochimica Polonica is an OpenAccess quarterly and publishes four issues a year. All contents are distributed under the Creative Commons Attribution-ShareAlike 4.0 International (CC BY 4.0) license. Everybody may use the content following terms: Attribution — You must give appropriate credit, provide a link to the license, and indicate if changes were made. You may do so in any reasonable manner, but not in any way that suggests the licensor endorses you or your use.