[Immobilization of the glutathione by the complementary coordination binding].

A simple method for immobilization of biologically imporant molecules with many functional fragments by selective binding of their thiogroups with the surface caroxyl groups by cadmium ions was proposed. Biofunctional properties of these structures were studied by surface plasmon resonance method on the model of the glutathione (GSH), which was immobilized by means of mixed (a:b form 1:100 o 1:700) thiol monolayers with terminal groups of the methyl/hydroxyl (b) and carboxyl (a) type. The maintenance of the biofunctional conformation ofglutathione-S-transferase (GST) after its interaction with GSH was checked by the use of specific anti-GST antibodies. It was shown that CH3 matrix has considerable non-specific binding and is not suitable for the formation of the biofunctional GST layer. At the same time OH-based structures demonstrate specific interaction GST-anti-GST, the stoichiometry of which corresponds to the bidentate binding. Considered simple method of the immobilization can be used to create the functional surface architectures in the analyticasl biochemistry and chemical analysis.