Study of Cd2+ complexation by the glutathione fragments Cys-Gly (CG) and gamma-Glu-Cys (gamma-EC) by differential pulse polarography.
A differential pulse polarographic study of the Cd2+/gamma-Glu-Cys and Cd2+/Cys-Gly systems assisted by the alternating least-squares multivariate curve resolution (MCR-ALS) method was carried out to obtain a better understanding of the different metal affinities of the complexation sites on glutathione (GSH). The simultaneous analysis of the titration of peptide with metal and of metal with peptide allowed the resolution of the Cd2+/Cys-Gly system, whereas in the analysis of the Cd2+/gamma-Glu-Cys system the analysis of a single titration experiment was sufficient. The analysis of the shape of the resulting pure voltammograms and concentration profiles of the resolved components suggested the presence of two different types of bound Cd2+ in the two systems considered, that could be attributed to Cd2+ bound to one or two sulfur atoms to form complexes of stoichiometry 1:1 and 1:2. respectively.
Cruz-Vásquez
Boris H
BH
Departament de Química Analitica, Universitat de Barcelona, Spain.
Diaz-Cruz
José Manuel
JM
Ariño
Cristina
C
Esteban
Miquel
M
Tauler
Romà
R