4-HYDROXYNONENAL INTERACTION WITH RHODOPSIN

4-Hydroxynonenal binds easily to rhodopsin and this was accompanied by a decrease in measurable sulfhydryl groups. Analysis of tryptic diges ts of the rhodopsin-HNE adduct by high performance liquid chromatograp hy 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 d esorption time of flight mass spectrometry showed that up to ten molec ules of HNE bound to rhodopsin. (C) 1997 Academic Press