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http://purl.uniprot.org/citations/3979555http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3979555http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3979555http://www.w3.org/2000/01/rdf-schema#comment"Cytosolic glutathione transferase was purified from human placenta and human liver. Three different forms of the enzyme were obtained, the acidic (pi), the near-neutral (mu), and the basic (alpha-epsilon) forms; two had free alpha-amino groups (pi, mu) and one had a blocked alpha-amino group (alpha-epsilon). N-terminal sequence analyses and total compositions gave clearly different results for each form, although transferases pi and mu showed 35% sequence homology in the N-terminal regions, with a 1-residue shift in starting position. Consequently, the proteins are concluded to be products of three discrete but related genes."xsd:string
http://purl.uniprot.org/citations/3979555http://purl.org/dc/terms/identifier"doi:10.1016/0014-5793(85)80324-0"xsd:string
http://purl.uniprot.org/citations/3979555http://purl.org/dc/terms/identifier"doi:10.1016/0014-5793(85)80324-0"xsd:string
http://purl.uniprot.org/citations/3979555http://purl.uniprot.org/core/author"Joernvall H."xsd:string
http://purl.uniprot.org/citations/3979555http://purl.uniprot.org/core/author"Joernvall H."xsd:string
http://purl.uniprot.org/citations/3979555http://purl.uniprot.org/core/author"Mannervik B."xsd:string
http://purl.uniprot.org/citations/3979555http://purl.uniprot.org/core/author"Mannervik B."xsd:string
http://purl.uniprot.org/citations/3979555http://purl.uniprot.org/core/author"Alin P."xsd:string
http://purl.uniprot.org/citations/3979555http://purl.uniprot.org/core/author"Alin P."xsd:string
http://purl.uniprot.org/citations/3979555http://purl.uniprot.org/core/date"1985"xsd:gYear
http://purl.uniprot.org/citations/3979555http://purl.uniprot.org/core/date"1985"xsd:gYear
http://purl.uniprot.org/citations/3979555http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/3979555http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/3979555http://purl.uniprot.org/core/pages"319-322"xsd:string
http://purl.uniprot.org/citations/3979555http://purl.uniprot.org/core/pages"319-322"xsd:string
http://purl.uniprot.org/citations/3979555http://purl.uniprot.org/core/title"Structural evidence for three different types of glutathione transferase in human tissues."xsd:string
http://purl.uniprot.org/citations/3979555http://purl.uniprot.org/core/title"Structural evidence for three different types of glutathione transferase in human tissues."xsd:string
http://purl.uniprot.org/citations/3979555http://purl.uniprot.org/core/volume"182"xsd:string
http://purl.uniprot.org/citations/3979555http://purl.uniprot.org/core/volume"182"xsd:string
http://purl.uniprot.org/citations/3979555http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/3979555
http://purl.uniprot.org/citations/3979555http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/3979555
http://purl.uniprot.org/citations/3979555http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/3979555
http://purl.uniprot.org/citations/3979555http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/3979555