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. 1979 Jan 1;177(1):215–223. doi: 10.1042/bj1770215

Investigation of the organization of rhodopsin in the sheep photoreceptor membrane by using cross-linking reagents.

M Brett, J B Findlay
PMCID: PMC1186359  PMID: 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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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