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|
Bibliographical noteFunding Information:
This work was supported by a grant from the National Eye Institute (EY 08818) and by the Air Force Of®ce of Scienti®c Research, Air Force Systems Command, USAF, under Grant 93-NL036. The U.S. government is authorized to reproduce and distribute reprints for governmental purposes notwithstanding any copyright notation hereon. The author thanks Matt Rees for synthesis of HNE, Sharon Hapner for technical assistance, Dave Barnidge and Joe Sears for help with the time of ¯ight mass spectrometry, and James Lewis at UC Santa Cruz for assistance with isolation of the bovine rod outer segments. Dr. van Kuijk is a Research to Prevent Blindness William & Mary Greve Scholar.