Inactivation and conformational changes of fatty acid synthase from chicken liver during unfolding by sodium dodecyl sulfate.
Int J Biochem Cell Biol
; 30(12): 1319-30, 1998 Dec.
Article
en En
| MEDLINE
| ID: mdl-9924801
ABSTRACT
Fatty acid synthase is an important enzyme participating in energy metabolism in vivo. The inactivation and conformational changes of the multifunctional fatty acid synthase from chicken liver in SDS solutions have been studied. The results show that the denaturation of this multifunctional enzyme by SDS occurred in three stages. At low concentrations of SDS (less than 0.15 mM) the enzyme was completely inactivated with regard to the overall reaction. For each component of the enzyme, the loss of activity occurred at higher concentrations of SDS. Significant conformational changes (as indicated by the changes of the intrinsic fluorescence emission and the ultraviolet difference spectra) occurred at higher concentrations of SDS. Increasing the SDS concentration caused only slight changes of the CD spectra, indicating that SDS had no significant effect on the secondary structure of the enzyme. The results suggest that the active sites of the multifunctional fatty acid synthase display more conformational flexibility than the enzyme molecule as a whole.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Dodecil Sulfato de Sodio
/
Tensoactivos
/
Pliegue de Proteína
/
Ácido Graso Sintasas
/
Hígado
Límite:
Animals
Idioma:
En
Revista:
Int J Biochem Cell Biol
Asunto de la revista:
BIOQUIMICA
Año:
1998
Tipo del documento:
Article