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http://purl.uniprot.org/citations/2448300http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2448300http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2448300http://www.w3.org/2000/01/rdf-schema#comment"Incubation of human plasma with 27 nM [gamma-32P]ATP in the presence of 20 mM MnCl2 results in the phosphorylation of several proteins detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography. About 60% of the incorporated radioactivity is found in a 75-kDa protein containing [32P] phosphoserine. The amino-terminal amino acid sequence of the purified 75-kDa [32P]phosphoprotein is identical to that of vitronectin (also termed serum spreading factor or complement S protein). Rabbit antiserum against vitronectin precipitates greater than 90% of the 75-kDa [32P]phosphoprotein from plasma. Reverse phase chromatography of [32P]vitronectin degraded sequentially with CNBr and chymotrypsin yields one major labeled peptide. The sequence of the peptide, Ser-Arg-Arg-Pro-[32PO4]Ser-Arg-Ala-Thr, corresponds to residues 374-381 which are located in the heparin-binding fragment of vitronectin identified by Suzuki et al. [1984) J. Biol. Chem. 259, 15307-15314). Vitronectin could potentially be phosphorylated in vivo with ATP released from injured cells or secreted by platelets activated during hemostasis."xsd:string
http://purl.uniprot.org/citations/2448300http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(19)77969-1"xsd:string
http://purl.uniprot.org/citations/2448300http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(19)77969-1"xsd:string
http://purl.uniprot.org/citations/2448300http://purl.uniprot.org/core/author"Siegel N.R."xsd:string
http://purl.uniprot.org/citations/2448300http://purl.uniprot.org/core/author"Siegel N.R."xsd:string
http://purl.uniprot.org/citations/2448300http://purl.uniprot.org/core/author"Inhorn R.C."xsd:string
http://purl.uniprot.org/citations/2448300http://purl.uniprot.org/core/author"Inhorn R.C."xsd:string
http://purl.uniprot.org/citations/2448300http://purl.uniprot.org/core/author"Tollefsen D.M."xsd:string
http://purl.uniprot.org/citations/2448300http://purl.uniprot.org/core/author"Tollefsen D.M."xsd:string
http://purl.uniprot.org/citations/2448300http://purl.uniprot.org/core/author"McGuire E.A."xsd:string
http://purl.uniprot.org/citations/2448300http://purl.uniprot.org/core/author"McGuire E.A."xsd:string
http://purl.uniprot.org/citations/2448300http://purl.uniprot.org/core/author"Peacock M.E."xsd:string
http://purl.uniprot.org/citations/2448300http://purl.uniprot.org/core/author"Peacock M.E."xsd:string
http://purl.uniprot.org/citations/2448300http://purl.uniprot.org/core/date"1988"xsd:gYear
http://purl.uniprot.org/citations/2448300http://purl.uniprot.org/core/date"1988"xsd:gYear
http://purl.uniprot.org/citations/2448300http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/2448300http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/2448300http://purl.uniprot.org/core/pages"1942-1945"xsd:string
http://purl.uniprot.org/citations/2448300http://purl.uniprot.org/core/pages"1942-1945"xsd:string
http://purl.uniprot.org/citations/2448300http://purl.uniprot.org/core/title"Phosphorylation of vitronectin by a protein kinase in human plasma. Identification of a unique phosphorylation site in the heparin-binding domain."xsd:string
http://purl.uniprot.org/citations/2448300http://purl.uniprot.org/core/title"Phosphorylation of vitronectin by a protein kinase in human plasma. Identification of a unique phosphorylation site in the heparin-binding domain."xsd:string
http://purl.uniprot.org/citations/2448300http://purl.uniprot.org/core/volume"263"xsd:string
http://purl.uniprot.org/citations/2448300http://purl.uniprot.org/core/volume"263"xsd:string