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http://purl.uniprot.org/citations/3038855http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3038855http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3038855http://www.w3.org/2000/01/rdf-schema#comment"The cDNA fragments corresponding to the domains with four consecutive E-F hand structures in the large and small subunits of chicken and rabbit calcium-activated neutral protease (CANP) were inserted into an expression vector (pUC8 or pUC18). The resulting plasmids were used to transform E. coli, and isopropyl-1-thio-beta-D-galactoside (IPTG)-inducible expression was performed. The resulting four kinds of E-F hand structure-domains (the chicken large subunit, rabbit high- and low-calcium-requiring large subunits, and rabbit small subunit) were purified and analyzed for their calcium-binding abilities and capacities by the microscale filter assay. Most of the E-F hand structures could bind calcium and 2 or 4 mol of Ca2+ ions bound to the four consecutive E-F hand structures. The calcium-binding affinity of the E-F hand structures in the large subunit roughly corresponds to the calcium concentration required for its CANP activity."xsd:string
http://purl.uniprot.org/citations/3038855http://purl.org/dc/terms/identifier"doi:10.1093/oxfordjournals.jbchem.a121956"xsd:string
http://purl.uniprot.org/citations/3038855http://purl.org/dc/terms/identifier"doi:10.1093/oxfordjournals.jbchem.a121956"xsd:string
http://purl.uniprot.org/citations/3038855http://purl.uniprot.org/core/author"Minami Y."xsd:string
http://purl.uniprot.org/citations/3038855http://purl.uniprot.org/core/author"Minami Y."xsd:string
http://purl.uniprot.org/citations/3038855http://purl.uniprot.org/core/author"Suzuki K."xsd:string
http://purl.uniprot.org/citations/3038855http://purl.uniprot.org/core/author"Suzuki K."xsd:string
http://purl.uniprot.org/citations/3038855http://purl.uniprot.org/core/author"Kawasaki H."xsd:string
http://purl.uniprot.org/citations/3038855http://purl.uniprot.org/core/author"Kawasaki H."xsd:string
http://purl.uniprot.org/citations/3038855http://purl.uniprot.org/core/author"Emori Y."xsd:string
http://purl.uniprot.org/citations/3038855http://purl.uniprot.org/core/author"Emori Y."xsd:string
http://purl.uniprot.org/citations/3038855http://purl.uniprot.org/core/date"1987"xsd:gYear
http://purl.uniprot.org/citations/3038855http://purl.uniprot.org/core/date"1987"xsd:gYear
http://purl.uniprot.org/citations/3038855http://purl.uniprot.org/core/name"J. Biochem."xsd:string
http://purl.uniprot.org/citations/3038855http://purl.uniprot.org/core/name"J. Biochem."xsd:string
http://purl.uniprot.org/citations/3038855http://purl.uniprot.org/core/pages"889-895"xsd:string
http://purl.uniprot.org/citations/3038855http://purl.uniprot.org/core/pages"889-895"xsd:string
http://purl.uniprot.org/citations/3038855http://purl.uniprot.org/core/title"E-F hand structure-domain of calcium-activated neutral protease (CANP) can bind Ca2+ ions."xsd:string
http://purl.uniprot.org/citations/3038855http://purl.uniprot.org/core/title"E-F hand structure-domain of calcium-activated neutral protease (CANP) can bind Ca2+ ions."xsd:string
http://purl.uniprot.org/citations/3038855http://purl.uniprot.org/core/volume"101"xsd:string
http://purl.uniprot.org/citations/3038855http://purl.uniprot.org/core/volume"101"xsd:string
http://purl.uniprot.org/citations/3038855http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/3038855
http://purl.uniprot.org/citations/3038855http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/3038855