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http://purl.uniprot.org/citations/2328317http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2328317http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2328317http://www.w3.org/2000/01/rdf-schema#comment"Fibrinogen Baltimore III, a congenital abnormal fibrinogen with impaired fibrin monomer polymerization, displays a normal gamma-chain and a gamma-variant that has an apparently lower relative molecular weight (mol wt) than normal on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Reverse phase high-performance liquid chromatography (HPLC) analysis of the lysyl endopeptidase digest of the purified gamma-chains of fibrinogen Baltimore III revealed the presence of a peptide that is not found in the digest of the normal fibrinogen gamma-chain. Amino acid sequence analysis of this peptide indicated that the gamma-chain residue 308, asparagine, is replaced by isoleucine. Concanavalin A bound both normal and variant gamma-chains of fibrinogen Baltimore III, indicating that the carbohydrate moiety is not altered and is not responsible for the increase in electrophoretic mobility of the Baltimore III gamma-chain. This study suggests that the integrity of gamma Asn308 is critical for fibrin monomer polymerization, since alteration to either a basic (fibrinogen Kyoto I, Asn----Lys) or hydrophobic (Asn----Ile) residue results in significantly delayed polymerization of fibrinogen to fibrin."xsd:string
http://purl.uniprot.org/citations/2328317http://purl.uniprot.org/core/author"Dang C.V."xsd:string
http://purl.uniprot.org/citations/2328317http://purl.uniprot.org/core/author"Dang C.V."xsd:string
http://purl.uniprot.org/citations/2328317http://purl.uniprot.org/core/author"Bantia S."xsd:string
http://purl.uniprot.org/citations/2328317http://purl.uniprot.org/core/author"Bantia S."xsd:string
http://purl.uniprot.org/citations/2328317http://purl.uniprot.org/core/author"Bell W.R."xsd:string
http://purl.uniprot.org/citations/2328317http://purl.uniprot.org/core/author"Bell W.R."xsd:string
http://purl.uniprot.org/citations/2328317http://purl.uniprot.org/core/date"1990"xsd:gYear
http://purl.uniprot.org/citations/2328317http://purl.uniprot.org/core/date"1990"xsd:gYear
http://purl.uniprot.org/citations/2328317http://purl.uniprot.org/core/name"Blood"xsd:string
http://purl.uniprot.org/citations/2328317http://purl.uniprot.org/core/name"Blood"xsd:string
http://purl.uniprot.org/citations/2328317http://purl.uniprot.org/core/pages"1659-1663"xsd:string
http://purl.uniprot.org/citations/2328317http://purl.uniprot.org/core/pages"1659-1663"xsd:string
http://purl.uniprot.org/citations/2328317http://purl.uniprot.org/core/title"Polymerization defect of fibrinogen Baltimore III due to a gamma Asn308-->Ile mutation."xsd:string
http://purl.uniprot.org/citations/2328317http://purl.uniprot.org/core/title"Polymerization defect of fibrinogen Baltimore III due to a gamma Asn308-->Ile mutation."xsd:string
http://purl.uniprot.org/citations/2328317http://purl.uniprot.org/core/volume"75"xsd:string
http://purl.uniprot.org/citations/2328317http://purl.uniprot.org/core/volume"75"xsd:string
http://purl.uniprot.org/citations/2328317http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2328317
http://purl.uniprot.org/citations/2328317http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2328317
http://purl.uniprot.org/citations/2328317http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/2328317
http://purl.uniprot.org/citations/2328317http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/2328317
http://purl.uniprot.org/uniprot/P02679http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/2328317
http://purl.uniprot.org/uniprot/P02679#attribution-98AE7581014F47E2CC9A8A76E3CA6774http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/2328317