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http://purl.uniprot.org/citations/3745199http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3745199http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3745199http://www.w3.org/2000/01/rdf-schema#comment"Rabbit reticulocyte eukaryotic initiation factor 2 was phosphorylated with the heme-regulated alpha subunit of eukaryotic initiation factor 2 kinase, and then the individual subunits were resolved by reversed-phase high performance liquid chromatography. Phosphorylated and unphosphorylated forms of the alpha subunit also were well resolved. The NH2-terminal sequences of intact alpha and gamma subunits were determined. No sequence was obtained from the beta subunit, suggesting that it may have a blocked NH2-terminus. Overlapping tryptic and chymotryptic phosphopeptides from the NH2-terminal sequence of the alpha subunit of eukaryotic initiation factor 2 were used to establish the order of amino acids 1-52 and localized the phosphorylation site within the sequence: -Leu-Leu-Ser48-Glu-Leu-Ser51-. Subdigestion of a tryptic fragment with chymotrypsin generated only phosphopeptides that appeared to terminate at leucine 50, indicating phosphorylation at serine 48."xsd:string
http://purl.uniprot.org/citations/3745199http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(18)67107-8"xsd:string
http://purl.uniprot.org/citations/3745199http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(18)67107-8"xsd:string
http://purl.uniprot.org/citations/3745199http://purl.uniprot.org/core/author"Wettenhall R.E.H."xsd:string
http://purl.uniprot.org/citations/3745199http://purl.uniprot.org/core/author"Wettenhall R.E.H."xsd:string
http://purl.uniprot.org/citations/3745199http://purl.uniprot.org/core/author"Kudlicki W."xsd:string
http://purl.uniprot.org/citations/3745199http://purl.uniprot.org/core/author"Kudlicki W."xsd:string
http://purl.uniprot.org/citations/3745199http://purl.uniprot.org/core/author"Kramer G."xsd:string
http://purl.uniprot.org/citations/3745199http://purl.uniprot.org/core/author"Kramer G."xsd:string
http://purl.uniprot.org/citations/3745199http://purl.uniprot.org/core/author"Hardesty B."xsd:string
http://purl.uniprot.org/citations/3745199http://purl.uniprot.org/core/author"Hardesty B."xsd:string
http://purl.uniprot.org/citations/3745199http://purl.uniprot.org/core/date"1986"xsd:gYear
http://purl.uniprot.org/citations/3745199http://purl.uniprot.org/core/date"1986"xsd:gYear
http://purl.uniprot.org/citations/3745199http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/3745199http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/3745199http://purl.uniprot.org/core/pages"12444-12447"xsd:string
http://purl.uniprot.org/citations/3745199http://purl.uniprot.org/core/pages"12444-12447"xsd:string
http://purl.uniprot.org/citations/3745199http://purl.uniprot.org/core/title"The NH2-terminal sequence of the alpha and gamma subunits of eukaryotic initiation factor 2 and the phosphorylation site for the heme-regulated eIF-2 alpha kinase."xsd:string
http://purl.uniprot.org/citations/3745199http://purl.uniprot.org/core/title"The NH2-terminal sequence of the alpha and gamma subunits of eukaryotic initiation factor 2 and the phosphorylation site for the heme-regulated eIF-2 alpha kinase."xsd:string
http://purl.uniprot.org/citations/3745199http://purl.uniprot.org/core/volume"261"xsd:string
http://purl.uniprot.org/citations/3745199http://purl.uniprot.org/core/volume"261"xsd:string
http://purl.uniprot.org/citations/3745199http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/3745199
http://purl.uniprot.org/citations/3745199http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/3745199