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http://purl.uniprot.org/citations/2470348http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2470348http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2470348http://www.w3.org/2000/01/rdf-schema#comment"A full-length cDNA clone for the 13-14 kDa soluble beta-galactoside-binding lectin was isolated from a bovine fibroblast cDNA library. The derived amino acid sequence shows eight differences from a preliminary partial amino acid sequence given previously for the bovine heart lectin. This observation led to a re-examination of the data and correction of the heart lectin protein sequence. Except for a possible polymorphism of the heart lectin at position 57, the fibroblast and heart lectin sequences are considered identical. The epitope recognized by two monoclonal anti-(bovine lectin) antibodies, 36/8 and 9/5, was identified as the tetrapeptide sequence W-G-A/S-E/D by the isolation of several different cDNA clones from a human intestine cDNA library. A similar tetrapeptide is present in all of the soluble beta-galactoside-binding animal lectins sequenced thus far. It is also found in myelin basic protein, which we show is antigenically cross-reactive with the lectin. In myelin basic protein the tetrapeptide is a part of the major domain previously shown to be responsible for the induction of experimental allergic encephalomyelitis."xsd:string
http://purl.uniprot.org/citations/2470348http://purl.org/dc/terms/identifier"doi:10.1042/bj2590283"xsd:string
http://purl.uniprot.org/citations/2470348http://purl.org/dc/terms/identifier"doi:10.1042/bj2590283"xsd:string
http://purl.uniprot.org/citations/2470348http://purl.uniprot.org/core/author"Feizi T."xsd:string
http://purl.uniprot.org/citations/2470348http://purl.uniprot.org/core/author"Feizi T."xsd:string
http://purl.uniprot.org/citations/2470348http://purl.uniprot.org/core/author"Abbott W.M."xsd:string
http://purl.uniprot.org/citations/2470348http://purl.uniprot.org/core/author"Abbott W.M."xsd:string
http://purl.uniprot.org/citations/2470348http://purl.uniprot.org/core/author"Edwards Y."xsd:string
http://purl.uniprot.org/citations/2470348http://purl.uniprot.org/core/author"Edwards Y."xsd:string
http://purl.uniprot.org/citations/2470348http://purl.uniprot.org/core/author"Mellor A."xsd:string
http://purl.uniprot.org/citations/2470348http://purl.uniprot.org/core/author"Mellor A."xsd:string
http://purl.uniprot.org/citations/2470348http://purl.uniprot.org/core/date"1989"xsd:gYear
http://purl.uniprot.org/citations/2470348http://purl.uniprot.org/core/date"1989"xsd:gYear
http://purl.uniprot.org/citations/2470348http://purl.uniprot.org/core/name"Biochem. J."xsd:string
http://purl.uniprot.org/citations/2470348http://purl.uniprot.org/core/name"Biochem. J."xsd:string
http://purl.uniprot.org/citations/2470348http://purl.uniprot.org/core/pages"283-290"xsd:string
http://purl.uniprot.org/citations/2470348http://purl.uniprot.org/core/pages"283-290"xsd:string
http://purl.uniprot.org/citations/2470348http://purl.uniprot.org/core/title"Soluble bovine galactose-binding lectin. cDNA cloning reveals the complete amino acid sequence and an antigenic relationship with the major encephalitogenic domain of myelin basic protein."xsd:string
http://purl.uniprot.org/citations/2470348http://purl.uniprot.org/core/title"Soluble bovine galactose-binding lectin. cDNA cloning reveals the complete amino acid sequence and an antigenic relationship with the major encephalitogenic domain of myelin basic protein."xsd:string
http://purl.uniprot.org/citations/2470348http://purl.uniprot.org/core/volume"259"xsd:string
http://purl.uniprot.org/citations/2470348http://purl.uniprot.org/core/volume"259"xsd:string
http://purl.uniprot.org/citations/2470348http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2470348
http://purl.uniprot.org/citations/2470348http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2470348