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http://purl.uniprot.org/citations/12951322http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12951322http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12951322http://www.w3.org/2000/01/rdf-schema#comment"Opticin is a class III member of the extracellular matrix small leucine-rich repeat protein (SLRP) family that was initially identified in the eye in association with the collagen fibrils of the vitreous humor. Recombinant and tissue-extracted forms of bovine opticin were subjected to biochemical and biophysical characterization. Following SDS-PAGE the predominant component produced by both forms was a broad band between 45-52 kDa. There was evidence for two-stage processing and, additionally, a proteolytic cleavage product of approximately 25 kDa. Deconvolution of circular dichroism spectra revealed beta-sheet (41%), beta-turn (21%), and alpha-helix (10%), and thermal denaturation experiments showed a transition with a midpoint of 47 degrees C. Weight-averaged molecular mass measurements using both light scattering and analytical ultracentrifugation demonstrated that opticin exists in solution as a stable dimer of approximately 90 kDa, which can be dissociated into a monomer by denaturation with 2.5 m guanidine hydrochloride or during SDS-polyacrylamide electrophoresis. Opticin remains a dimer after removal of the amino-terminal region by O-sialoglycoprotein endopeptidase digestion, suggesting that dimer formation is mediated by the leucine-rich repeats. Dimerization could have a number of functional consequences, including divalent ligand interactions."xsd:string
http://purl.uniprot.org/citations/12951322http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m303117200"xsd:string
http://purl.uniprot.org/citations/12951322http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m303117200"xsd:string
http://purl.uniprot.org/citations/12951322http://purl.uniprot.org/core/author"Jowitt T.A."xsd:string
http://purl.uniprot.org/citations/12951322http://purl.uniprot.org/core/author"Jowitt T.A."xsd:string
http://purl.uniprot.org/citations/12951322http://purl.uniprot.org/core/author"Hindson V.J."xsd:string
http://purl.uniprot.org/citations/12951322http://purl.uniprot.org/core/author"Hindson V.J."xsd:string
http://purl.uniprot.org/citations/12951322http://purl.uniprot.org/core/author"Bishop P.N."xsd:string
http://purl.uniprot.org/citations/12951322http://purl.uniprot.org/core/author"Bishop P.N."xsd:string
http://purl.uniprot.org/citations/12951322http://purl.uniprot.org/core/author"Scott P.G."xsd:string
http://purl.uniprot.org/citations/12951322http://purl.uniprot.org/core/author"Scott P.G."xsd:string
http://purl.uniprot.org/citations/12951322http://purl.uniprot.org/core/author"Le Goff M.M."xsd:string
http://purl.uniprot.org/citations/12951322http://purl.uniprot.org/core/author"Le Goff M.M."xsd:string
http://purl.uniprot.org/citations/12951322http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12951322http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12951322http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12951322http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12951322http://purl.uniprot.org/core/pages"45280-45287"xsd:string
http://purl.uniprot.org/citations/12951322http://purl.uniprot.org/core/pages"45280-45287"xsd:string
http://purl.uniprot.org/citations/12951322http://purl.uniprot.org/core/title"Characterization of opticin and evidence of stable dimerization in solution."xsd:string
http://purl.uniprot.org/citations/12951322http://purl.uniprot.org/core/title"Characterization of opticin and evidence of stable dimerization in solution."xsd:string
http://purl.uniprot.org/citations/12951322http://purl.uniprot.org/core/volume"278"xsd:string
http://purl.uniprot.org/citations/12951322http://purl.uniprot.org/core/volume"278"xsd:string