Characterization of an hexapeptide containing three thiol groups by HPLC - Optimization of parameters
The hexapeptide Lys-Cys-Thr-Cys-Cys-Ala [56-61] MTI (TF) is a molecule intrinsic to the metallothionein structure. Its chromatographic behaviour on a reverse phase column, using electrochemical detection, has been studied in order to get a better understanding of its chemical stability under various conditions. The optimisation procedure of the HPLC method is presented. Different major parameters such as percentage of organic solvent, pH of the mobile phase and flow of the elution have been systematically changed. The optimal hydrodynamic voltammogram has been established, leading to the selection of an efficient potential for the electrochemical detection based on the oxidation of the thiol group. The basic chromatogram of the peptide obtained with the selected separation parameters consists of two peaks. The relative proportion of these two peaks can evoluate depending on experimental conditions. This leads to formulation of a hypothesis in which the fully reduced form and a partially oxidised form of the peptide with intramolecular disulphide bridge, co-exist.
Bibliographic Reference: Paper presented: 38th International Symposium on Analysis of Peptides, Stockholm (SE), June 2-4, 1993
Availability: Available from (1) as Paper EN 37515 ORA
Record Number: 199310854 / Last updated on: 1994-11-29
Original language: en
Available languages: en