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http://purl.uniprot.org/citations/2828054http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2828054http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2828054http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/2828054http://www.w3.org/2000/01/rdf-schema#comment"1. Diacylglycerol kinase apoprotein was purified from membranes of Escherichia coli K12 by a six-step procedure that included HPLC. The proposed assignment of the enzyme to the dgkA gene [Lightner et al. (1983) J. Biol. Chem. 258, 10856-10861] could be supported by molecular mass determination (approximately 14 kDa), N-terminal sequencing (Met-Ala-Asn), cyanogen bromide fragmentation and amino acid analysis. As predicted, proline was absent. 2. The membrane-associated as well as the butan-1-ol-dissolved enzyme survived heating to 100 degrees C. 3. Alkylglycoside detergents were found to constitute an additional class of lipid activators. 4. The enzyme apoprotein in a non-activating substrate/detergent solution was capable of autocatalytic self-activation which was attributed to a novel feedback activation mechanism involving phosphatidic acid (diacylglycerol 3-phosphate)."xsd:string
http://purl.uniprot.org/citations/2828054http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1988.tb13795.x"xsd:string
http://purl.uniprot.org/citations/2828054http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1988.tb13795.x"xsd:string
http://purl.uniprot.org/citations/2828054http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1988.tb13795.x"xsd:string
http://purl.uniprot.org/citations/2828054http://purl.uniprot.org/core/author"Sandermann H. Jr."xsd:string
http://purl.uniprot.org/citations/2828054http://purl.uniprot.org/core/author"Sandermann H. Jr."xsd:string
http://purl.uniprot.org/citations/2828054http://purl.uniprot.org/core/author"Kaiser U."xsd:string
http://purl.uniprot.org/citations/2828054http://purl.uniprot.org/core/author"Kaiser U."xsd:string
http://purl.uniprot.org/citations/2828054http://purl.uniprot.org/core/author"Russ E."xsd:string
http://purl.uniprot.org/citations/2828054http://purl.uniprot.org/core/author"Russ E."xsd:string
http://purl.uniprot.org/citations/2828054http://purl.uniprot.org/core/date"1988"xsd:gYear
http://purl.uniprot.org/citations/2828054http://purl.uniprot.org/core/date"1988"xsd:gYear
http://purl.uniprot.org/citations/2828054http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/2828054http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/2828054http://purl.uniprot.org/core/pages"335-342"xsd:string
http://purl.uniprot.org/citations/2828054http://purl.uniprot.org/core/pages"335-342"xsd:string
http://purl.uniprot.org/citations/2828054http://purl.uniprot.org/core/title"Lipid-dependent membrane enzymes. Purification to homogeneity and further characterization of diacylglycerol kinase from Escherichia coli."xsd:string
http://purl.uniprot.org/citations/2828054http://purl.uniprot.org/core/title"Lipid-dependent membrane enzymes. Purification to homogeneity and further characterization of diacylglycerol kinase from Escherichia coli."xsd:string
http://purl.uniprot.org/citations/2828054http://purl.uniprot.org/core/volume"171"xsd:string
http://purl.uniprot.org/citations/2828054http://purl.uniprot.org/core/volume"171"xsd:string
http://purl.uniprot.org/citations/2828054http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2828054
http://purl.uniprot.org/citations/2828054http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2828054