FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1541738754> ?p ?o ?g. }

• W1541738754 endingPage "22539" @default.
• W1541738754 startingPage "22531" @default.
• W1541738754 abstract "The assembly of macromolecular complexes containing factors Xa and Va on suitable phospholipid surfaces is crucial for rapid activation of prothrombin. We have used quantitative affinity chromatography to characterize the interaction between factor Va and intact factor Xa on the one hand and between factor Va and factor Xa lacking the gamma-carboxyglutamic acid (Gla)-containing module on the other. The dissociation constants were found to be 1.0 +/- 0.1 and 9.5 +/- 1.8 microM, respectively. There was good agreement between these dissociation constants and the concentrations of active site-inhibited factor Xa and Gla-domainless factor Xa that caused half-maximal inhibition of prothrombin activation. To investigate whether the noncatalytic modules of factor Xa interacted directly with factor Va, intact modules were isolated from proteolytic digests of factor X and used as inhibitors of prothrombin activation. The inhibitory effect observed with the isolated Gla module in the absence of phospholipid was due to inhibition of the amidolytic activity of factor Xa rather than to an interaction with factor Va. The epidermal growth factor-like modules did not inhibit prothrombin activation. Using antibodies specific for calcium-dependent epitopes in the serine protease module of factor Xa we demonstrated that Ca2+ binding to the Gla module alters the conformation of the catalytic module. Half-maximal binding was observed at approximately 0.8 mM Ca2+. Evidence was also obtained for the presence of two Gla-independent Ca(2+)-binding sites in factor Xa. One of these sites, located in the NH2-terminal epidermal growth factor-like module, was half-saturated at approximately 60 microM Ca2+ in intact factor Xa and at approximately 1.2 mM Ca2+ in Gla-domainless factor Xa. This site appeared not to influence the conformation of the protease module. The second site, which was half-saturated at approximately 0.16 mM Ca2+, appeared to reside in the serine protease module and to alter its conformation as judged by binding of antibodies specific for calcium-dependent epitopes." @default.
• W1541738754 created "2016-06-24" @default.
• W1541738754 creator A5004228898 @default.
• W1541738754 creator A5048301059 @default.
• W1541738754 creator A5088062100 @default.
• W1541738754 date "1993-10-01" @default.
• W1541738754 modified "2023-09-30" @default.
• W1541738754 title "Effects of Ca2+ binding on the protease module of factor Xa and its interaction with factor Va. Evidence for two Gla-independent Ca(2+)-binding sites in factor Xa." @default.
• W1541738754 cites W1479704195 @default.
• W1541738754 cites W1479925054 @default.
• W1541738754 cites W1483113783 @default.
• W1541738754 cites W1484991497 @default.
• W1541738754 cites W1488254260 @default.
• W1541738754 cites W1493544534 @default.
• W1541738754 cites W1502744283 @default.
• W1541738754 cites W1505723334 @default.
• W1541738754 cites W1508750197 @default.
• W1541738754 cites W1512258266 @default.
• W1541738754 cites W1514670886 @default.
• W1541738754 cites W1519085965 @default.
• W1541738754 cites W1526553788 @default.
• W1541738754 cites W1531765158 @default.
• W1541738754 cites W1533471204 @default.
• W1541738754 cites W1533611871 @default.
• W1541738754 cites W1534532061 @default.
• W1541738754 cites W1539709480 @default.
• W1541738754 cites W1554329457 @default.
• W1541738754 cites W1556087419 @default.
• W1541738754 cites W1559899200 @default.
• W1541738754 cites W1561534093 @default.
• W1541738754 cites W1563102421 @default.
• W1541738754 cites W1564829539 @default.
• W1541738754 cites W1569301169 @default.
• W1541738754 cites W1569452935 @default.
• W1541738754 cites W1580349070 @default.
• W1541738754 cites W1589293066 @default.
• W1541738754 cites W1589621417 @default.
• W1541738754 cites W1595615359 @default.
• W1541738754 cites W1603661744 @default.
• W1541738754 cites W1603783662 @default.
• W1541738754 cites W1604706922 @default.
• W1541738754 cites W1654405751 @default.
• W1541738754 cites W1786757590 @default.
• W1541738754 cites W1840736997 @default.
• W1541738754 cites W1865475665 @default.
• W1541738754 cites W1926616884 @default.
• W1541738754 cites W1961597147 @default.
• W1541738754 cites W1973308700 @default.
• W1541738754 cites W1984445610 @default.
• W1541738754 cites W1985228189 @default.
• W1541738754 cites W2002262647 @default.
• W1541738754 cites W2009759103 @default.
• W1541738754 cites W2017569531 @default.
• W1541738754 cites W2037383079 @default.
• W1541738754 cites W2041349540 @default.
• W1541738754 cites W2056871814 @default.
• W1541738754 cites W2066902897 @default.
• W1541738754 cites W2072252524 @default.
• W1541738754 cites W2090530842 @default.
• W1541738754 cites W2094344554 @default.
• W1541738754 cites W2097803943 @default.
• W1541738754 cites W2153423854 @default.
• W1541738754 cites W2156393985 @default.
• W1541738754 cites W2170055916 @default.
• W1541738754 cites W2212388653 @default.
• W1541738754 cites W2402295418 @default.
• W1541738754 cites W2417964224 @default.
• W1541738754 cites W62994428 @default.
• W1541738754 cites W87735197 @default.
• W1541738754 cites W953289541 @default.
• W1541738754 cites W975870285 @default.
• W1541738754 doi "https://doi.org/10.1016/s0021-9258(18)41562-1" @default.
• W1541738754 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8226763" @default.
• W1541738754 hasPublicationYear "1993" @default.
• W1541738754 type Work @default.
• W1541738754 sameAs 1541738754 @default.
• W1541738754 citedByCount "44" @default.
• W1541738754 countsByYear W15417387542014 @default.
• W1541738754 countsByYear W15417387542015 @default.
• W1541738754 crossrefType "journal-article" @default.
• W1541738754 hasAuthorship W1541738754A5004228898 @default.
• W1541738754 hasAuthorship W1541738754A5048301059 @default.
• W1541738754 hasAuthorship W1541738754A5088062100 @default.
• W1541738754 hasBestOaLocation W15417387541 @default.
• W1541738754 hasConcept C107824862 @default.
• W1541738754 hasConcept C12554922 @default.
• W1541738754 hasConcept C181199279 @default.
• W1541738754 hasConcept C185592680 @default.
• W1541738754 hasConcept C199360897 @default.
• W1541738754 hasConcept C203014093 @default.
• W1541738754 hasConcept C2776714187 @default.
• W1541738754 hasConcept C2777292125 @default.
• W1541738754 hasConcept C2777444498 @default.
• W1541738754 hasConcept C2781039887 @default.
• W1541738754 hasConcept C41008148 @default.
• W1541738754 hasConcept C55493867 @default.
• W1541738754 hasConcept C86803240 @default.
• W1541738754 hasConcept C89560881 @default.

• next