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http://purl.uniprot.org/citations/9497332http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9497332http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9497332http://www.w3.org/2000/01/rdf-schema#comment"Reported here is the isolation and characterization of two antibacterial peptides synthesized in an ant Myrmecia gulosa in response to bacterial challenge. The peptides were purified by reversed-phase high performance liquid chromatography and characterized by peptide sequencing and mass spectrometry. Both peptides were formed from 16 amino acids, were rich in proline ( approximately 30%), and had N-acetylgalactosamine O-linked to a conserved threonine. The activity of a synthetic non-glycosylated isoform was markedly reduced demonstrating that glycosylation was necessary for maximum activity. The peptides were active only against growing Escherichia coli. They were inactive against stationary cells, Gram-positive bacteria, the yeast Candida albicans, two species of mammalian cells, and bovine pestivirus."xsd:string
http://purl.uniprot.org/citations/9497332http://purl.org/dc/terms/identifier"doi:10.1074/jbc.273.11.6139"xsd:string
http://purl.uniprot.org/citations/9497332http://purl.org/dc/terms/identifier"doi:10.1074/jbc.273.11.6139"xsd:string
http://purl.uniprot.org/citations/9497332http://purl.uniprot.org/core/author"Gooley A.A."xsd:string
http://purl.uniprot.org/citations/9497332http://purl.uniprot.org/core/author"Gooley A.A."xsd:string
http://purl.uniprot.org/citations/9497332http://purl.uniprot.org/core/author"Beattie A.J."xsd:string
http://purl.uniprot.org/citations/9497332http://purl.uniprot.org/core/author"Beattie A.J."xsd:string
http://purl.uniprot.org/citations/9497332http://purl.uniprot.org/core/author"Mackintosh J.A."xsd:string
http://purl.uniprot.org/citations/9497332http://purl.uniprot.org/core/author"Mackintosh J.A."xsd:string
http://purl.uniprot.org/citations/9497332http://purl.uniprot.org/core/author"Veal D.A."xsd:string
http://purl.uniprot.org/citations/9497332http://purl.uniprot.org/core/author"Veal D.A."xsd:string
http://purl.uniprot.org/citations/9497332http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9497332http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9497332http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9497332http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9497332http://purl.uniprot.org/core/pages"6139-6143"xsd:string
http://purl.uniprot.org/citations/9497332http://purl.uniprot.org/core/pages"6139-6143"xsd:string
http://purl.uniprot.org/citations/9497332http://purl.uniprot.org/core/title"Isolation from an ant Myrmecia gulosa of two inducible O-glycosylated proline-rich antibacterial peptides."xsd:string
http://purl.uniprot.org/citations/9497332http://purl.uniprot.org/core/title"Isolation from an ant Myrmecia gulosa of two inducible O-glycosylated proline-rich antibacterial peptides."xsd:string
http://purl.uniprot.org/citations/9497332http://purl.uniprot.org/core/volume"273"xsd:string
http://purl.uniprot.org/citations/9497332http://purl.uniprot.org/core/volume"273"xsd:string
http://purl.uniprot.org/citations/9497332http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9497332
http://purl.uniprot.org/citations/9497332http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9497332