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http://purl.uniprot.org/citations/1704366http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1704366http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1704366http://www.w3.org/2000/01/rdf-schema#comment"The interaction between type 1 plasminogen activator inhibitor (PAI-1) and fragments of vitronectin (Vn) was investigated. The PAI-1-binding domain was not destroyed when Vn was cleaved by treatment with either acid or CNBr. Acid-cleaved Vn was fractionated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and analyzed by PAI-1 ligand binding. The smallest fragment (Mr 40,000) that retained PAI-1 binding function was sequenced and shown to contain the NH2 terminus of the molecule. Further cleavage of this fragment by treatment with CNBr generated a Mr 35,000 fragment (Pro52-Asp239) that did not interact with PAI-1, and a Mr 6,000 NH2-terminal fragment (Asp1-Met51) that spanned the somatomedin B domain and contained the RGD (cell binding) sequence. The purified Mr 6,000 fragment competed with immobilized Vn for PAI-1 binding, and formed complexes with activated PAI-1. These complexes could be immunoprecipitated by antibodies to PAI-1. Synthetic peptides containing the RGD sequence had no effect on the binding of this fragment to PAI-1. These results suggest that the cell-binding and PAI-1 binding sequences of Vn occupy distinct regions in the NH2-terminal somatomedin B domain of the molecule."xsd:string
http://purl.uniprot.org/citations/1704366http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(18)49921-8"xsd:string
http://purl.uniprot.org/citations/1704366http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(18)49921-8"xsd:string
http://purl.uniprot.org/citations/1704366http://purl.uniprot.org/core/author"Loskutoff D.J."xsd:string
http://purl.uniprot.org/citations/1704366http://purl.uniprot.org/core/author"Loskutoff D.J."xsd:string
http://purl.uniprot.org/citations/1704366http://purl.uniprot.org/core/author"Seiffert D."xsd:string
http://purl.uniprot.org/citations/1704366http://purl.uniprot.org/core/author"Seiffert D."xsd:string
http://purl.uniprot.org/citations/1704366http://purl.uniprot.org/core/date"1991"xsd:gYear
http://purl.uniprot.org/citations/1704366http://purl.uniprot.org/core/date"1991"xsd:gYear
http://purl.uniprot.org/citations/1704366http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/1704366http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/1704366http://purl.uniprot.org/core/pages"2824-2830"xsd:string
http://purl.uniprot.org/citations/1704366http://purl.uniprot.org/core/pages"2824-2830"xsd:string
http://purl.uniprot.org/citations/1704366http://purl.uniprot.org/core/title"Evidence that type 1 plasminogen activator inhibitor binds to the somatomedin B domain of vitronectin."xsd:string
http://purl.uniprot.org/citations/1704366http://purl.uniprot.org/core/title"Evidence that type 1 plasminogen activator inhibitor binds to the somatomedin B domain of vitronectin."xsd:string
http://purl.uniprot.org/citations/1704366http://purl.uniprot.org/core/volume"266"xsd:string
http://purl.uniprot.org/citations/1704366http://purl.uniprot.org/core/volume"266"xsd:string
http://purl.uniprot.org/citations/1704366http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1704366
http://purl.uniprot.org/citations/1704366http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1704366
http://purl.uniprot.org/citations/1704366http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/1704366
http://purl.uniprot.org/citations/1704366http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/1704366
http://purl.uniprot.org/uniprot/P04004http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/1704366
http://purl.uniprot.org/uniprot/P04004#attribution-17F27008283F9E221C7AC1603F87068Fhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/1704366