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dc.contributor.authorWeiss, Ellen R.
dc.contributor.authorKelleher, Daniel J.
dc.contributor.authorJohnson, Gary L.
dc.date2022-08-11T08:10:05.000
dc.date.accessioned2022-08-23T16:54:41Z
dc.date.available2022-08-23T16:54:41Z
dc.date.issued1988-05-05
dc.date.submitted2008-08-15
dc.identifier.citationJ Biol Chem. 1988 May 5;263(13):6150-4.
dc.identifier.issn0021-9258 (Print)
dc.identifier.pmid3283122
dc.identifier.urihttp://hdl.handle.net/20.500.14038/42556
dc.description.abstractSite-directed antipeptide antibodies generated against the predicted cytoplasmic sequences of rhodopsin were used to map the binding domains for transducin, the retinal G-protein, on the photoreceptor. Antibodies against synthetic peptides corresponding to loop 3-4, loop 5-6, and the serine/threonine-rich region of the COOH terminus recognize rhodopsin by immunoblot analysis and also recognize the native protein within the membrane, allowing these probes to be used for functional studies. Rhodopsin reconstituted into phospholipid vesicles binds transducin in the light which significantly reduces the binding of antipeptide antibodies corresponding to loop 3-4 and the COOH terminus of rhodopsin. However, the binding of the antibody raised against a 14-amino-acid peptide corresponding to a sequence within loop 5-6 of rhodopsin was unaffected by the presence of transducin. These results suggest a preferential involvement of regions in or near loop 3-4 and the COOH terminus in the binding of transducin to rhodopsin. In contrast, a significant portion of loop 5-6 does not form a binding domain for the G-protein.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=3283122&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://www.jbc.org/cgi/reprint/263/13/6150
dc.subjectAnimals
dc.subject*Antibodies
dc.subjectBinding Sites
dc.subjectImmunosorbent Techniques
dc.subjectMembrane Proteins
dc.subjectRabbits
dc.subjectRetinal Pigments
dc.subjectRhodopsin
dc.subjectTransducin
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleMapping sites of interaction between rhodopsin and transducin using rhodopsin antipeptide antibodies
dc.typeJournal Article
dc.source.journaltitleThe Journal of biological chemistry
dc.source.volume263
dc.source.issue13
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/894
dc.identifier.contextkey579783
html.description.abstract<p>Site-directed antipeptide antibodies generated against the predicted cytoplasmic sequences of rhodopsin were used to map the binding domains for transducin, the retinal G-protein, on the photoreceptor. Antibodies against synthetic peptides corresponding to loop 3-4, loop 5-6, and the serine/threonine-rich region of the COOH terminus recognize rhodopsin by immunoblot analysis and also recognize the native protein within the membrane, allowing these probes to be used for functional studies. Rhodopsin reconstituted into phospholipid vesicles binds transducin in the light which significantly reduces the binding of antipeptide antibodies corresponding to loop 3-4 and the COOH terminus of rhodopsin. However, the binding of the antibody raised against a 14-amino-acid peptide corresponding to a sequence within loop 5-6 of rhodopsin was unaffected by the presence of transducin. These results suggest a preferential involvement of regions in or near loop 3-4 and the COOH terminus in the binding of transducin to rhodopsin. In contrast, a significant portion of loop 5-6 does not form a binding domain for the G-protein.</p>
dc.identifier.submissionpathoapubs/894
dc.contributor.departmentDepartment of Biochemistry
dc.source.pages6150-4


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