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 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.
van Kuijk
F J
FJ
Department of Ophthalmology and Visual Sciences, University of Texas Medical Branch, Galveston 77555-1067, USA.
D000447:Aldehydes / Q000737:chemistry* / Q000494:pharmacology; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D003432:Cross-Linking Reagents; D004228:Dithionitrobenzoic Acid; D013058:Mass Spectrometry; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification; D012243:Rhodopsin / Q000737:chemistry* / Q000187:drug effects; D013438:Sulfhydryl Compounds / Q000032:analysis; D014357:Trypsin
D000447:Aldehydes; D003432:Cross-Linking Reagents; D010446:Peptide Fragments; D013438:Sulfhydryl Compounds; D012243:Rhodopsin; D004228:Dithionitrobenzoic Acid; D014357:Trypsin; C027576:4-hydroxy-2-nonenal