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- W145524097 abstract "The authors previously described two human monoclonal antibodies (MAbs) which inactivated factor V. The authors have now purified the predominant antibody (H2) on protein A Sepharose using a pH gradient and typed it as IgG/sub 1/,. Immunoprecipitation of /sup 125/I-human factor Va with H2 demonstrated specificity for the heavy chain (D), Mr = 105,000. The authors compared using ELISA the competitive binding to factor Va, of H2, H1 and two mouse MAbs, B38 (directed to E) and B10 (to activation peptide, Cl). All four antibodies recognized distinct epitopes in factor V with steric overlap in some cases. Factor Xa showed a concentration dependent competition for binding of H1, H2 and B38 but not B10 to factor V/Va in ELISA. All MAbs bound to factor V/Va in the absence of Ca/sup + +/. However, Ca/sup + +/ at 8 mM increased the binding of H1 and H2 to 165% and 360% and did not have any effect on the binding of either mouse MAbs. Prothrombin at a concentration of up to 400 ..mu..g/ml did not inhibit binding of any of these antibodies. Thus, both the light (E) and heavy (D) chains of factor Va but not the activation peptide (Cl) interactmore » with factor Xa as defined by the MAbs. In addition, sites on both chains for Ca/sup + +/ are recognized by particular MAbs (H1 and H2). These studies increase their knowledge of the interactions of factor V domains in the formation of prothrombinase complex.« less" @default.
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- W145524097 date "1986-05-01" @default.
- W145524097 modified "2023-09-23" @default.
- W145524097 title "Epitope mapping of functional domains of human factor V with human and mouse monoclonal antibodies" @default.
- W145524097 hasPublicationYear "1986" @default.
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