| Popis: |
The SERS spectrum of anti-human immunoglobulin G alkaline phosphatase conjugate (anti-IgG) adsorbed on a silver electrode was observed as a function of potential and buffer ionic strength. SERS was capable of characterizing molecular rearrangements at the electrode surface due to the electrochemical reduction of the disulfide bonds in cystine amino acid groups. Electrode coverage of the anti-IgG decreased as the ionic strength was raised, coinciding with apparent denaturation of the protein. Compared with earlier electrochemical and quartz crystal microbalance (QCM) studies, which also detected interfacial changes with reduction [E.S. Grabbe, R.P. Buck and O.R. Melroy, J. Electroanal. Chem., 223 (1987) 67], the SERS data were superior for describing differences in coverage and surface restructuring that were previously observed. |
