4-Hydroxynonenal binds easily to rhodopsin and this was accompanied by a decrease in measurable sulfhydryl groups. Analysis of tryptic digests of the rhodopsin-HNE adduct by high performance liquid chromatography revealed that several peptides present in the digests of rhodopsin disappeared, whereas HNE modified peptides not originally present were found in digests of the rhodopsin-HNE adduct. Matrix assisted laser desorption time of flight mass spectrometry showed that up to ten molecules of HNE bound to rhodopsin.
|Original language||English (US)|
|Number of pages||5|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Jan 13 1997|