Abstract
This chapter discusses the proteolysis of rhodopsin. Proteases have been valuable probes of the structure of many membrane proteins. Limited proteolysis of bovine rhodopsin has revealed information about the location of specific sites along the polypeptide sequence, about the organization of rhodopsin in natural and reconstituted membranes, and about conformational changes induced by light. Proteolysis of rhodopsin in disk membranes may be used to help localize any newly described marker in the rhodopsin polypeptide. It has been observed that at higher ratios of subtilisin to rhodopsin, a third discrete cleavage site may be exposed within F1, permitting higher resolution mapping. Most exciting is the possibility that excision of extradiskal portions of rhodopsin can be used to localize regions of interaction between rhodopsin and the light-activated enzymes of the rod outer segment.
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