RESUMO
Cyclic voltammetry has been applied for the characterization of cross-linked horse heart cytochrome c (HHC) on cysteamine-modified gold electrodes. The cross-linking, i.e. amide bond formation, between the proteins was achieved by using 1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide (EDC) as coupling reagent. The optimal conditions for the formation of the HHC film were determined by varying the HHC concentration. In addition the reproducibility, stability and the influence of the scan rate upon these films were investigated with cyclic voltammetry. The protein film stability in a 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (HEPES) buffer solution was tested by UV/vis absorption spectroscopy.
Assuntos
Citocromos c/química , Eletrodos/normas , Animais , Reagentes de Ligações Cruzadas , Cisteamina , Eletroquímica/métodos , Eletroquímica/normas , Etildimetilaminopropil Carbodi-Imida , Ouro , Cavalos , Reprodutibilidade dos Testes , Análise EspectralRESUMO
The application of ozonization and cyclic voltammetry for the regeneration of gold chips containing a chemisorbed gelatin layer is reported. The efficiency of the regeneration process was analyzed using various surface analysis techniques indicating a complete removal of the biopolymer layer. The current findings open up perspectives for regeneration and multiple application of gold chips for SPR measurements.
