| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1245390 | Talanta | 2008 | 5 Pages |
Abstract
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.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Karolien De Wael, Hans Buschop, Lina De Smet, Annemie Adriaens,