Immobilization of cytochrome c on cysteamine-modified gold electrodes with EDC as coupling agent.
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.
De Wael
Karolien
K
Ghent University, Department of Analytical Chemistry, Krijgslaan 281 S12, B-9000 Ghent, Belgium.
Buschop
Hans
H
De Smet
Lina
L
Adriaens
Annemie
A
D000818:Animals; D003432:Cross-Linking Reagents; D003543:Cysteamine; D045304:Cytochromes c / Q000737:chemistry*; D004563:Electrochemistry / Q000379:methods / Q000592:standards; D004566:Electrodes / Q000592:standards*; D005022:Ethyldimethylaminopropyl Carbodiimide; D006046:Gold; D006736:Horses; D015203:Reproducibility of Results; D013057:Spectrum Analysis
D003432:Cross-Linking Reagents; D003543:Cysteamine; D006046:Gold; D045304:Cytochromes c; D005022:Ethyldimethylaminopropyl Carbodiimide