Investigation of the Organization of Rhodopsin in the Sheep Photoreceptor Membrane by Using Cross-linking Reagents

Overview

Journal Biochem J

Specialty Biochemistry

Date 1979 Jan 1

PMID 106845

Citations 11

Authors

M Brett

J B Findlay

Affiliations

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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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