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  • Title: Investigation of the organization of rhodopsin in the sheep photoreceptor membrane by using cross-linking reagents.
    Author: Brett M, Findlay JB.
    Journal: Biochem J; 1979 Jan 01; 177(1):215-23. PubMed ID: 106845.
    Abstract:
    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.
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