Investigation of the organization of rhodopsin in the sheep photoreceptor membrane by using cross-linking reagents.
The organization of rhodopsin in the photoreceptor membrane of sheep rod outer segments was investigated by using a variety of bifunctional reagents. Of the nine reagents used, seven gave oligomeric opsin species, whereas two, copper phenanthroline and dithiobisphenyl azide, failed to cross-link the protein. In general, the cross-linked species obtained showed diminishing yields from dimer to tetramer, together with some higher-molecular-weight aggregates. It is proposed that the patterns of cross-linking arise as a result of collision complexes and best describe a monomeric organization for native rhodopsin. No significant differences between the patterns obtained with dark-adapted bleached or regenerated protein states were observed. This interpretation is discussed in relation to the postulated mechanism of action of rhodopsin.
D000818:Animals; D002462:Cell Membrane / Q000032:analysis; D003902:Detergents; D004139:Dinitrofluorobenzene / Q000031:analogs & derivatives; D004591:Electrophoresis, Polyacrylamide Gel; D005976:Glutaral; D007094:Imides; D046911:Macromolecular Substances; D010618:Phenanthrolines; D010786:Photoreceptor Cells / Q000032:analysis*; D012168:Retinal Pigments; D012243:Rhodopsin; D012756:Sheep
D003902:Detergents; D007094:Imides; D046911:Macromolecular Substances; D010618:Phenanthrolines; D012168:Retinal Pigments; D012243:Rhodopsin; D004139:Dinitrofluorobenzene; D005976:Glutaral