Matches in SemOpenAlex for { <https://semopenalex.org/work/W2011521805> ?p ?o ?g. }
Showing items 1 to 93 of
93
with 100 items per page.
- W2011521805 endingPage "973" @default.
- W2011521805 startingPage "965" @default.
- W2011521805 abstract "The coagulation factor IX/factor X-binding protein (IX/X-bp) from the venom of Trimeresurus flavoviridis is a heterogeneous two-chain protein, and the structure of each chain is similar to that of the carbohydrate-recognition domain of C-type lectins, such as asialoglycoprotein receptors, pancreatic stone protein, and the Feɛ receptor for immunoglobulin E. Analysis of the binding properties of IX/X-bp revealed that it binds to the γ-carboxyglutamic acid (Gla)-containing domains of factors IX and X [Atoda, H. et al. (1994) Eur. J. Biochem. 224, 703–708]. In the present study, we isolated another anticoagulant protein that binds to factor IX but it is not to factor X. This protein, designated IX-bp, inhibited factor IXa-induced clotting but not factor Xa-induced clotting, whereas IX/X-bp inhibits both. The concentration of IX-bp for half-maximal binding to solid-phase bovine factor IX was 0.4 nM whereas IX-bp did not bind to factor X even at 40 nM. The binding of IX-bp to solid-phase factor IX was inhibited by the addition of Gla-domain peptide of factor IX, indicating that IX-bp binds to the Gla-domain region of factor IX. IX-bp had two Ca2+-binding sites with different affinities for Ca2+ ions. At pH 7.5, the apparent Kd values for these sites were 14 and 130 μM, respectively. IX-bp was a two-chain protein (27.5-kDa band before reduction and 16.8- and 15.7-kDa bands after reduction on SDS-PAGE) and it reacted with immunoglobulin G against IX/X-bp. The complete amino acid sequence of IX-bp was determined. The 16.8-kDa chain (A chain) of IX-bp consisted of 129 residues, of which 19 were different from those in the A chain of IX/X-bp (129 residues). The sequence of the 15.7-kDa chain (B chain) was identical to that of the B chain of IX/X-bp (123 residues). We conclude that IX-bp is a protein that is structurally similar to but functionally different from IX/X-bp. The difference of binding specificity between IX-bp and IX/X-bp presumably arises from the sequence differences in the A chains." @default.
- W2011521805 created "2016-06-24" @default.
- W2011521805 creator A5012840606 @default.
- W2011521805 creator A5041729199 @default.
- W2011521805 creator A5054837831 @default.
- W2011521805 creator A5058488316 @default.
- W2011521805 creator A5076671641 @default.
- W2011521805 date "1995-10-01" @default.
- W2011521805 modified "2023-09-25" @default.
- W2011521805 title "Blood Coagulation Factor IX-Binding Protein from the Venom of Trimeresurus flavoviridis: Purification and Characterization" @default.
- W2011521805 doi "https://doi.org/10.1093/jb/118.5.965" @default.
- W2011521805 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8749314" @default.
- W2011521805 hasPublicationYear "1995" @default.
- W2011521805 type Work @default.
- W2011521805 sameAs 2011521805 @default.
- W2011521805 citedByCount "59" @default.
- W2011521805 countsByYear W20115218052012 @default.
- W2011521805 countsByYear W20115218052013 @default.
- W2011521805 countsByYear W20115218052014 @default.
- W2011521805 countsByYear W20115218052017 @default.
- W2011521805 countsByYear W20115218052018 @default.
- W2011521805 countsByYear W20115218052019 @default.
- W2011521805 countsByYear W20115218052020 @default.
- W2011521805 crossrefType "journal-article" @default.
- W2011521805 hasAuthorship W2011521805A5012840606 @default.
- W2011521805 hasAuthorship W2011521805A5041729199 @default.
- W2011521805 hasAuthorship W2011521805A5054837831 @default.
- W2011521805 hasAuthorship W2011521805A5058488316 @default.
- W2011521805 hasAuthorship W2011521805A5076671641 @default.
- W2011521805 hasConcept C104317684 @default.
- W2011521805 hasConcept C107824862 @default.
- W2011521805 hasConcept C118552586 @default.
- W2011521805 hasConcept C126322002 @default.
- W2011521805 hasConcept C153911025 @default.
- W2011521805 hasConcept C15744967 @default.
- W2011521805 hasConcept C185592680 @default.
- W2011521805 hasConcept C186738567 @default.
- W2011521805 hasConcept C203014093 @default.
- W2011521805 hasConcept C2777292125 @default.
- W2011521805 hasConcept C2777444498 @default.
- W2011521805 hasConcept C2778382381 @default.
- W2011521805 hasConcept C2780930249 @default.
- W2011521805 hasConcept C2781221834 @default.
- W2011521805 hasConcept C2910886357 @default.
- W2011521805 hasConcept C2992139802 @default.
- W2011521805 hasConcept C553089730 @default.
- W2011521805 hasConcept C55493867 @default.
- W2011521805 hasConcept C71924100 @default.
- W2011521805 hasConcept C86803240 @default.
- W2011521805 hasConcept C89560881 @default.
- W2011521805 hasConceptScore W2011521805C104317684 @default.
- W2011521805 hasConceptScore W2011521805C107824862 @default.
- W2011521805 hasConceptScore W2011521805C118552586 @default.
- W2011521805 hasConceptScore W2011521805C126322002 @default.
- W2011521805 hasConceptScore W2011521805C153911025 @default.
- W2011521805 hasConceptScore W2011521805C15744967 @default.
- W2011521805 hasConceptScore W2011521805C185592680 @default.
- W2011521805 hasConceptScore W2011521805C186738567 @default.
- W2011521805 hasConceptScore W2011521805C203014093 @default.
- W2011521805 hasConceptScore W2011521805C2777292125 @default.
- W2011521805 hasConceptScore W2011521805C2777444498 @default.
- W2011521805 hasConceptScore W2011521805C2778382381 @default.
- W2011521805 hasConceptScore W2011521805C2780930249 @default.
- W2011521805 hasConceptScore W2011521805C2781221834 @default.
- W2011521805 hasConceptScore W2011521805C2910886357 @default.
- W2011521805 hasConceptScore W2011521805C2992139802 @default.
- W2011521805 hasConceptScore W2011521805C553089730 @default.
- W2011521805 hasConceptScore W2011521805C55493867 @default.
- W2011521805 hasConceptScore W2011521805C71924100 @default.
- W2011521805 hasConceptScore W2011521805C86803240 @default.
- W2011521805 hasConceptScore W2011521805C89560881 @default.
- W2011521805 hasIssue "5" @default.
- W2011521805 hasLocation W20115218051 @default.
- W2011521805 hasLocation W20115218052 @default.
- W2011521805 hasOpenAccess W2011521805 @default.
- W2011521805 hasPrimaryLocation W20115218051 @default.
- W2011521805 hasRelatedWork W1717444018 @default.
- W2011521805 hasRelatedWork W1849352096 @default.
- W2011521805 hasRelatedWork W1994714114 @default.
- W2011521805 hasRelatedWork W2025905012 @default.
- W2011521805 hasRelatedWork W2029576247 @default.
- W2011521805 hasRelatedWork W2048599158 @default.
- W2011521805 hasRelatedWork W2063199350 @default.
- W2011521805 hasRelatedWork W2473782998 @default.
- W2011521805 hasRelatedWork W4240625035 @default.
- W2011521805 hasRelatedWork W55237838 @default.
- W2011521805 hasVolume "118" @default.
- W2011521805 isParatext "false" @default.
- W2011521805 isRetracted "false" @default.
- W2011521805 magId "2011521805" @default.
- W2011521805 workType "article" @default.