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http://purl.uniprot.org/citations/9354636http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9354636http://www.w3.org/2000/01/rdf-schema#comment"The oligomeric state of the Na/Ca-K exchanger in the plasma membrane of bovine photoreceptors was investigated using chemical cross-linking techniques. In the natural membrane, virtually all Na/Ca-K exchanger could be cross-linked mainly to a complex having an apparent molecular mass of 490 kDa by cupric phenanthroline catalyzed disulfide bonding as evidenced by Western blotting. Stable cross-links of the exchanger were also obtained with the thiol-specific reagent N,N'-p-phenylidenedimaleimide. Neuraminidase treatment reduced the apparent molecular mass of the highly glycosylated Na/Ca-K exchanger and of the 490 kDa cross-link product by 50 and 85 kDa, respectively. DL-1,4-Bismaleimido-2,3-butanediol (BMBD), a novel cleavable dimaleimide, was synthesized in order to produce cross-links that were stable to reductive conditions. Purification of the BMBD cross-linked exchanger followed by two-dimensional SDS polyacrylamide electrophoresis identified the cross-linked homodimers of the exchanger. There was no indication of higher oligomers, suggesting that the exchanger exists as a dimer in the plasma membrane. Hydrodynamic properties of the detergent-solubilized exchanger were determined by velocity sedimentation and gel filtration chromatography. The Triton X-100-solubilized exchanger ran as a single species having a Stokes radius of 10.0 nm, a sedimentation coefficient of 5.4 S, and a partial specific volume of 0.74 mL/g in Triton X-100. Similar results were obtained for the CHAPS-solubilized exchanger. A molecular mass of 236 and 205 kDa was calculated for the exchanger-detergent complex and the detergent-free protein, respectively. Neuraminidase treatment further reduced the molecular mass of the exchanger indicating that glycosylation contributes significantly to the mass of the exchanger. Cross-links of the exchanger were not detected if cross-linking was attempted after solubilization in 10 mM CHAPS. However, after reconstitution of the purified exchanger into soybean phosphatidylcholine vesicles, chemical cross-linking yielded again dimers. On the basis of these cross-linking and hydrodynamic studies, we conclude that the exchanger exists as a homodimer in the rod outer segment plasma membrane but dissociates into a monomer when solubilized in detergent."xsd:string
http://purl.uniprot.org/citations/9354636http://purl.org/dc/terms/identifier"doi:10.1021/bi9710232"xsd:string
http://purl.uniprot.org/citations/9354636http://purl.uniprot.org/core/author"Molday R.S."xsd:string
http://purl.uniprot.org/citations/9354636http://purl.uniprot.org/core/author"Hagen V."xsd:string
http://purl.uniprot.org/citations/9354636http://purl.uniprot.org/core/author"Kim T.S."xsd:string
http://purl.uniprot.org/citations/9354636http://purl.uniprot.org/core/author"Schwarzer A."xsd:string
http://purl.uniprot.org/citations/9354636http://purl.uniprot.org/core/author"Bauer P.J."xsd:string
http://purl.uniprot.org/citations/9354636http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9354636http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/9354636http://purl.uniprot.org/core/pages"13667-13676"xsd:string
http://purl.uniprot.org/citations/9354636http://purl.uniprot.org/core/title"The Na/Ca-K exchanger of rod photoreceptor exists as dimer in the plasma membrane."xsd:string
http://purl.uniprot.org/citations/9354636http://purl.uniprot.org/core/volume"36"xsd:string
http://purl.uniprot.org/citations/9354636http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9354636
http://purl.uniprot.org/citations/9354636http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9354636
http://purl.uniprot.org/uniprot/#_O60721-mappedCitation-9354636http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/9354636
http://purl.uniprot.org/uniprot/O60721http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/9354636