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http://purl.uniprot.org/citations/1719959http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1719959http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1719959http://www.w3.org/2000/01/rdf-schema#comment"The bovine homologue of p65, a calmodulin-binding protein located in the membranes of synaptic vesicles and endocrine secretory granules, has been studied by the use of monoclonal antibodies directed against this antigen and against dopamine beta-mono-oxygenase. The protein (apparent molecular mass 67 kDa; pI = 5.5-6.2) is partially degraded by treatment with neuraminidase or endoglycosidase F. Trypsin treatment of intact adrenal chromaffin granules or of granule membranes releases a soluble 39 kDa fragment of p65 which corresponds to the whole of its cytoplasmic domain. This domain contains both the epitope for the monoclonal antibody cgm67 and the calmodulin-binding site. The 20 amino acids at the N-terminus of this fragment are identical to part of the rat p65 sequence."xsd:string
http://purl.uniprot.org/citations/1719959http://purl.org/dc/terms/identifier"doi:10.1042/bj2790699"xsd:string
http://purl.uniprot.org/citations/1719959http://purl.org/dc/terms/identifier"doi:10.1042/bj2790699"xsd:string
http://purl.uniprot.org/citations/1719959http://purl.uniprot.org/core/author"van Leeuwen F."xsd:string
http://purl.uniprot.org/citations/1719959http://purl.uniprot.org/core/author"van Leeuwen F."xsd:string
http://purl.uniprot.org/citations/1719959http://purl.uniprot.org/core/author"Haywood J."xsd:string
http://purl.uniprot.org/citations/1719959http://purl.uniprot.org/core/author"Haywood J."xsd:string
http://purl.uniprot.org/citations/1719959http://purl.uniprot.org/core/author"Tugal H.B."xsd:string
http://purl.uniprot.org/citations/1719959http://purl.uniprot.org/core/author"Tugal H.B."xsd:string
http://purl.uniprot.org/citations/1719959http://purl.uniprot.org/core/author"Phillips J.H."xsd:string
http://purl.uniprot.org/citations/1719959http://purl.uniprot.org/core/author"Phillips J.H."xsd:string
http://purl.uniprot.org/citations/1719959http://purl.uniprot.org/core/author"Apps D.K."xsd:string
http://purl.uniprot.org/citations/1719959http://purl.uniprot.org/core/author"Apps D.K."xsd:string
http://purl.uniprot.org/citations/1719959http://purl.uniprot.org/core/date"1991"xsd:gYear
http://purl.uniprot.org/citations/1719959http://purl.uniprot.org/core/date"1991"xsd:gYear
http://purl.uniprot.org/citations/1719959http://purl.uniprot.org/core/name"Biochem. J."xsd:string
http://purl.uniprot.org/citations/1719959http://purl.uniprot.org/core/name"Biochem. J."xsd:string
http://purl.uniprot.org/citations/1719959http://purl.uniprot.org/core/pages"699-703"xsd:string
http://purl.uniprot.org/citations/1719959http://purl.uniprot.org/core/pages"699-703"xsd:string
http://purl.uniprot.org/citations/1719959http://purl.uniprot.org/core/title"Glycosylation and transmembrane topography of bovine chromaffin granule p65."xsd:string
http://purl.uniprot.org/citations/1719959http://purl.uniprot.org/core/title"Glycosylation and transmembrane topography of bovine chromaffin granule p65."xsd:string
http://purl.uniprot.org/citations/1719959http://purl.uniprot.org/core/volume"279"xsd:string
http://purl.uniprot.org/citations/1719959http://purl.uniprot.org/core/volume"279"xsd:string