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- W305022647 abstract "The authors have previously reported the preparation of monoclonal antibodies that recognize various structural domains of factor XI. One antibody (5F7) is heavy chain specific, inhibited kaolin-mediated procoagulant activity 70%, had no effect on factor XI procoagulant activity and did not inhibit the release of a /sup 3/H-labeled activation peptide from factor IX by factor XIa. 5F7 also blocked high Mr kininogen binding to factor XI and the proteolytic activation of factor XI by factor XIIa in the presence of high Mr kininogen and kaolin. Peptide regions containing the high Mr kininogen binding site have been isolated using cyanogen bromide digests of factor XI which have been passed through a 5F7 antibody affinity columns. Further isolation of peptide regions containing the high Mr kininogen binding site was also achieved using high performance liquid chromatography. A 15,000 dalton peptide was isolated from a cyanogen bromide factor XI digest that is immunologically cross-reactive to the 5F7 antibody. The authors are currently analyzing this peptide by amino acid analysis and sequencing this peptide in order to place the high Mr kininogen binding domain within the known primary structure of the molecule." @default.
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- W305022647 date "1987-05-01" @default.
- W305022647 modified "2023-09-24" @default.
- W305022647 title "Identification and isolation of a peptide domain in the heavy chain region of factor XI that comprises the primary structure of the high Mr kininogen binding site" @default.
- W305022647 hasPublicationYear "1987" @default.
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