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Electrochemical study of the binding properties of a metallothionein I related peptide with cadmium or/and zinc
Author(s) -
Mendieta Jesús,
Rodríguez Adela Rosa
Publication year - 1996
Publication title -
electroanalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.574
H-Index - 128
eISSN - 1521-4109
pISSN - 1040-0397
DOI - 10.1002/elan.1140080514
Subject(s) - chemistry , cadmium , metallothionein , polarography , zinc , electrochemistry , stoichiometry , metal , inorganic chemistry , metal ions in aqueous solution , peptide , molecule , dissociation constant , dissociation (chemistry) , stability constants of complexes , ion , organic chemistry , electrode , biochemistry , receptor
Abstract An electrochemical study, using differential pulse polarography, of the binding properties of the peptide Lys‐Cys‐Thr‐Cys‐Cys‐Ala Thionein Fragment [56–61] MT I (FT) with cadmium and zinc was performed. This molecule, intrinsic to the metallothionein structure, was chosen as a model of the Cd, Zn Metallothioneins ion exchange and binding properties. The influence of the addition of metal ions, cadmium and/or zinc was studied with different ratios of complexing ligand/metallic cations, FT/M(II). It is assumed that the main complex M(II)‐FT possesses a stoichiometry of 1:1, but probably two or more complexes co‐exist depending on the FT/M ratios. The equilibrium M + FT ⇌ MFT concerning the complexation equilibrium of formation and dissociation was investigated as a function of pH, going from acid to basic solution and vice versa in different mixtures: Cd:FT, Zn:FT and Cd:Zn:FT. The apparent stability constants of the complexes Cd‐FT, Zn‐FT were estimated at different pH values.