Electrochemical behaviour of biological molecules intrinsic to metallothionein structure : Complexing properties of the peptidic fragment [56-61] MT with Cd and Zn
Metallothioneins (MT) are low molecular weight proteins which are characterised by a high cysteine content and a selective capacity to bind metal ions. The metal ions contained in these molecules are electroactive, as is the organic part of the MT (-SH groups). However, there has been little use of electrochemical techniques in the analysis of these molecules. In order to obtain a better understanding of the electrochemical behaviour of MT, a -SH containing compound, being part of the proteic structure, has been studied: the peptidic fragment Lys-Cys-Thr-Cys-Cys-Ala [56-61] MT I (FT). This peptide contains three cysteinyl residues which are considered as being the basic structural unit involved in binding one divalent ion. The electrochemical response of FT in the absence of metal ions was elucidated previously. The study on the influence of the addition of cadmium and zinc on the electrochemical response of FT is presented here using differential pulse polarography (DPP). The difference between the behaviour of FT in the presence or absence of Cd and Zn gives information about the complexing properties of this molecule with the aim of establishing analogies with MT characteristics.
Bibliographic Reference: Paper presented: EUROANALYSIS VIII, Edinburgh (GB), September 5-11, 1993
Availability: Available from (1) as Paper EN 37819 ORA
Record Number: 199311280 / Last updated on: 1994-11-29
Original language: en
Available languages: en