RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/241423http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/241423http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/241423http://www.w3.org/2000/01/rdf-schema#comment"1. Phospholipase C (EC 3.1.4.3) from Clostridium novyi (oedematiens) type A was purified 2000-fold by (NH4)2SO4 precipitation, DEAE-Sephadex treatment in a batchwise system and Sephadex G-100 column chromatography. 2. The purified preparation had a specific activity of 95 mumol per min per mg protein toward phosphatidylcholine. This preparation was free from protease, lipase and oxygen-labile delta-hemolysin. 3. Phosphatidylcholine was hydrolyzed at the highest rate, while sphingomyelin and lysophosphatidylcholine were hydrolyzed at much lower rates. 4. Sodium deoxycholate and divalent cations such as Mg2+ and Ca2+ were extremely effective in stimulating phosphatidylcholine-hydrolyzing activity of this enzyme. 5. This enzyme hemolyzed horse red cells by hydrolyzing phosphatidylcholine, spingomyelin and phosphatidylethanolamine."xsd:string
http://purl.uniprot.org/citations/241423http://purl.org/dc/terms/identifier"doi:10.1016/0005-2760(75)90082-x"xsd:string
http://purl.uniprot.org/citations/241423http://purl.org/dc/terms/identifier"doi:10.1016/0005-2760(75)90082-x"xsd:string
http://purl.uniprot.org/citations/241423http://purl.uniprot.org/core/author"Ikezawa H."xsd:string
http://purl.uniprot.org/citations/241423http://purl.uniprot.org/core/author"Ikezawa H."xsd:string
http://purl.uniprot.org/citations/241423http://purl.uniprot.org/core/author"Taguchi R."xsd:string
http://purl.uniprot.org/citations/241423http://purl.uniprot.org/core/author"Taguchi R."xsd:string
http://purl.uniprot.org/citations/241423http://purl.uniprot.org/core/date"1975"xsd:gYear
http://purl.uniprot.org/citations/241423http://purl.uniprot.org/core/date"1975"xsd:gYear
http://purl.uniprot.org/citations/241423http://purl.uniprot.org/core/name"Biochim. Biophys. Acta"xsd:string
http://purl.uniprot.org/citations/241423http://purl.uniprot.org/core/name"Biochim. Biophys. Acta"xsd:string
http://purl.uniprot.org/citations/241423http://purl.uniprot.org/core/pages"75-85"xsd:string
http://purl.uniprot.org/citations/241423http://purl.uniprot.org/core/pages"75-85"xsd:string
http://purl.uniprot.org/citations/241423http://purl.uniprot.org/core/title"Phospholipase C from Clostridium novyi type A. I."xsd:string
http://purl.uniprot.org/citations/241423http://purl.uniprot.org/core/title"Phospholipase C from Clostridium novyi type A. I."xsd:string
http://purl.uniprot.org/citations/241423http://purl.uniprot.org/core/volume"409"xsd:string
http://purl.uniprot.org/citations/241423http://purl.uniprot.org/core/volume"409"xsd:string
http://purl.uniprot.org/citations/241423http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/241423
http://purl.uniprot.org/citations/241423http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/241423
http://purl.uniprot.org/citations/241423http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/241423
http://purl.uniprot.org/citations/241423http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/241423
http://purl.uniprot.org/uniprot/Q46150http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/241423
http://purl.uniprot.org/uniprot/#_Q46150-citation-241423http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/241423