The structure of human apolipoprotein E2, E3 and E4 in solution. 2. Multidomain organization correlates with the stability of apoE structure.
Fiche publication
Date publication
janvier 2006
Auteurs
Membres identifiés du Cancéropôle Est :
Pr VISVIKIS Athanase
Tous les auteurs :
Clement-Collin V, Barbier A, Dergunov AD, Visvikis A, Siest G, Desmadril M, Takahashi M, Aggerbeck LP
Lien Pubmed
Résumé
The stabilities toward thermal and chemical denaturation of three recombinant isoforms of human apolipoprotein E (r-apoE2, r-apoE3 and r-apoE4), human plasma apoE3, the recombinant amino-terminal (NT) and the carboxyl-terminal (CT) domains of plasma apoE3 at pH 7 were studied using near and far ultraviolet circular dichroism (UV CD), fluorescence and size-exclusion chromatography. By far UV CD, thermal unfolding was irreversible for the intact apoE isoforms and consisted of a single transition. The r-apoE3 was found to be less stable as compared to the plasma protein and the stability of recombinant isoforms was r-apoE4
Référence
Biophys Chem. 2006 Jan 20;119(2):170-85