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http://purl.uniprot.org/citations/7599152http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7599152http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7599152http://www.w3.org/2000/01/rdf-schema#comment"Two high molecular mass proteins, flavocetin-A and flavocetin-B, were purified from Trimeresurus flavoviridis venom. On polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate, the apparent molecular mass of flavocetin-A and -B were 149 and 139 kDa, respectively, under nonreducing conditions. On reduction, flavocetin-A showed two distinct subunits (17 and 14 kDa), and flavocetin-B three distinct subunits (17, 15 and 14 kDa). At 1 microgram/ml, flavocetin-A and -B (flavocetins) inhibited the von Willebrand factor (vWF)-dependent aggregation of fixed human platelets. However, flavocetins (10 micrograms/ml) had no effect on ADP- and collagen-induced platelet aggregation in PRP. Flavocetins (3 micrograms/ml) also inhibited shear-induced platelet aggregation at high shear stress. Furthermore, flavocetin-A completely inhibited the aggregation of and ATP release from washed platelets stimulated with a low concentration of thrombin. Flavocetin-A specifically bound to platelet with high affinity (Kd = 0.35 +/-0.13 nM) at 21,500 +/-1760 binding sites per platelet. The N-terminal amino acid sequences of the subunits of flavocetin-A show a high degree of homology with those of echicetin, botrocetin, alboaggregin-B and factor IX/factor X-binding protein. These results suggest that flavocetins may be a useful tool for further investigation of the GPIb-vWF interaction."xsd:string
http://purl.uniprot.org/citations/7599152http://purl.org/dc/terms/identifier"doi:10.1016/0304-4165(95)00052-d"xsd:string
http://purl.uniprot.org/citations/7599152http://purl.org/dc/terms/identifier"doi:10.1016/0304-4165(95)00052-d"xsd:string
http://purl.uniprot.org/citations/7599152http://purl.uniprot.org/core/author"Suzuki M."xsd:string
http://purl.uniprot.org/citations/7599152http://purl.uniprot.org/core/author"Suzuki M."xsd:string
http://purl.uniprot.org/citations/7599152http://purl.uniprot.org/core/author"Satoh N."xsd:string
http://purl.uniprot.org/citations/7599152http://purl.uniprot.org/core/author"Satoh N."xsd:string
http://purl.uniprot.org/citations/7599152http://purl.uniprot.org/core/author"Sakai Y."xsd:string
http://purl.uniprot.org/citations/7599152http://purl.uniprot.org/core/author"Sakai Y."xsd:string
http://purl.uniprot.org/citations/7599152http://purl.uniprot.org/core/author"Kawasaki T."xsd:string
http://purl.uniprot.org/citations/7599152http://purl.uniprot.org/core/author"Kawasaki T."xsd:string
http://purl.uniprot.org/citations/7599152http://purl.uniprot.org/core/author"Titani K."xsd:string
http://purl.uniprot.org/citations/7599152http://purl.uniprot.org/core/author"Titani K."xsd:string
http://purl.uniprot.org/citations/7599152http://purl.uniprot.org/core/author"Takenaka T."xsd:string
http://purl.uniprot.org/citations/7599152http://purl.uniprot.org/core/author"Takenaka T."xsd:string
http://purl.uniprot.org/citations/7599152http://purl.uniprot.org/core/author"Fujimura Y."xsd:string
http://purl.uniprot.org/citations/7599152http://purl.uniprot.org/core/author"Fujimura Y."xsd:string
http://purl.uniprot.org/citations/7599152http://purl.uniprot.org/core/author"Taniuchi Y."xsd:string
http://purl.uniprot.org/citations/7599152http://purl.uniprot.org/core/author"Taniuchi Y."xsd:string
http://purl.uniprot.org/citations/7599152http://purl.uniprot.org/core/author"Kaku S."xsd:string
http://purl.uniprot.org/citations/7599152http://purl.uniprot.org/core/author"Kaku S."xsd:string
http://purl.uniprot.org/citations/7599152http://purl.uniprot.org/core/author"Hisamichi N."xsd:string
http://purl.uniprot.org/citations/7599152http://purl.uniprot.org/core/author"Hisamichi N."xsd:string