Publication details
Modification of horse heart cytochrome c with trans-2-hexenal
| Authors | |
|---|---|
| Year of publication | 1997 |
| Type | Article in Periodical |
| Magazine / Source | Chemical Research in Toxicology |
| MU Faculty or unit | |
| Citation | |
| Keywords | ELECTROOSMOTIC ZONE DISPLACEMENT; LIPID-PEROXIDATION PRODUCTS; BOVINESERUM-ALBUMIN; PROTEIN ADDUCTS; ALDEHYDES |
| Description | Horse heart cytochrome c reacting with trans-2-hexenal was used as a simple model of the nonspecific interactions of proteins with 2-alkenals. The reaction mixtures containing relatively high concentrations of the protein and aldehyde were characterized using visible spectrophotometry, fluorescence, and circular dichroism measurements, capillary isoelectric focusing, size-exclusion chromatography, polyacrylamide gel electrophoresis, and mass-spectrometric techniques. The mass-spectrometric data indicate that cytochrome c becomes modified with one or two molecules of hexenal as the major reaction product. The modified species with a correspondingly lowered isoelectric point were detected through capillary isoelectric focusing. The results of proteolytic studies indicate nonspecific modifications. Significant quantities of the oligomeric farms of hexenal-modified protein were also observed electrophoretically. |