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Stabilization of firefly luciferase against thermal stress by osmolytes.
- Source :
-
International journal of biological macromolecules [Int J Biol Macromol] 2008 Aug 15; Vol. 43 (2), pp. 187-91. Date of Electronic Publication: 2008 May 08. - Publication Year :
- 2008
-
Abstract
- The effects of osmolytes, including sucrose, sorbitol and proline on the remaining activity of firefly luciferase were measured. Heat inactivation studies showed that these osmolytes maintain the remaining activity of enzyme and increase activation energy of thermal unfolding reaction. Fluorescence and circular dichroism (CD) experiments showed changes in secondary and tertiary structure of firefly luciferase, in the presence of sucrose, sorbitol and proline. The unfolding curves of luciferase (obtained by far-UV CD spectra), indicated an irreversible thermal denaturation and raising of the midpoint of the unfolding transition temperature (T(m)) in the presence of osmolytes.
Details
- Language :
- English
- ISSN :
- 0141-8130
- Volume :
- 43
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- International journal of biological macromolecules
- Publication Type :
- Academic Journal
- Accession number :
- 18555523
- Full Text :
- https://doi.org/10.1016/j.ijbiomac.2008.05.001