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http://purl.uniprot.org/citations/2829172http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2829172http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2829172http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/2829172http://www.w3.org/2000/01/rdf-schema#comment"5-Lipoxygenase (EC 1.13.11.34), a Ca2+-and ATP-requiring enzyme, catalyzes the first two steps in the biosynthesis of the peptidoleukotrienes and the chemotactic factor leukotriene B4. A cDNA clone corresponding to 5-lipoxygenase was isolated from a human lung lambda gt11 expression library by immunoscreening with a polyclonal antibody. Additional clones from a human placenta lambda gt11 cDNA library were obtained by plaque hybridization with the 32P-labeled lung cDNA clone. Sequence data obtained from several overlapping clones indicate that the composite cDNAs contain the complete coding region for the enzyme. From the deduced primary structure, 5-lipoxygenase encodes a 673 amino acid protein with a calculated molecular weight of 77,839. Direct analysis of the native protein and its proteolytic fragments confirmed the deduced composition, the amino-terminal amino acid sequence, and the structure of many internal segments. 5-Lipoxygenase has no apparent sequence homology with leukotriene A4 hydrolase or Ca2+ -binding proteins. RNA blot analysis indicated substantial amounts of an mRNA species of approximately equal to 2700 nucleotides in leukocytes, lung, and placenta."xsd:string
http://purl.uniprot.org/citations/2829172http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/2829172http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/2829172http://purl.org/dc/terms/identifier"doi:10.1073/pnas.85.1.26"xsd:string
http://purl.uniprot.org/citations/2829172http://purl.org/dc/terms/identifier"doi:10.1073/pnas.85.1.26"xsd:string
http://purl.uniprot.org/citations/2829172http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2829172
http://purl.uniprot.org/citations/2829172http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2829172
http://purl.uniprot.org/citations/2829172http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2829172
http://purl.uniprot.org/citations/2829172http://purl.uniprot.org/core/author"Matsumoto T."xsd:string
http://purl.uniprot.org/citations/2829172http://purl.uniprot.org/core/author"Matsumoto T."xsd:string
http://purl.uniprot.org/citations/2829172http://purl.uniprot.org/core/author"Samuelsson B."xsd:string
http://purl.uniprot.org/citations/2829172http://purl.uniprot.org/core/author"Samuelsson B."xsd:string
http://purl.uniprot.org/citations/2829172http://purl.uniprot.org/core/author"Joernvall H."xsd:string
http://purl.uniprot.org/citations/2829172http://purl.uniprot.org/core/author"Joernvall H."xsd:string
http://purl.uniprot.org/citations/2829172http://purl.uniprot.org/core/author"Hoeoeg J.-O."xsd:string
http://purl.uniprot.org/citations/2829172http://purl.uniprot.org/core/author"Hoeoeg J.-O."xsd:string
http://purl.uniprot.org/citations/2829172http://purl.uniprot.org/core/author"Funk C.D."xsd:string
http://purl.uniprot.org/citations/2829172http://purl.uniprot.org/core/author"Funk C.D."xsd:string
http://purl.uniprot.org/citations/2829172http://purl.uniprot.org/core/author"Raadmark O."xsd:string
http://purl.uniprot.org/citations/2829172http://purl.uniprot.org/core/author"Raadmark O."xsd:string
http://purl.uniprot.org/citations/2829172http://purl.uniprot.org/core/date"1988"xsd:gYear
http://purl.uniprot.org/citations/2829172http://purl.uniprot.org/core/date"1988"xsd:gYear