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- W2992700530 abstract "A high titer, boost responding inhibitor was present in a patient and his nephew, both with severe hemophilia B. On digests of their DNA, Southern blots hybridized to a cDNA were normal. They had no detectable IX antigen, including immuno-radiometric assays with a calcium-requiring polyclonal antibody fraction, in either serum or urine (less than 0.03 U/dl). Plasmas from the patient and his nephew had 12 and 25 NIH U/ml inhibitor titers, respectively. They were fractionated over IX-agarose with calcium. Unlike fractionation of rabbit polyclonal antibodies, EDTA eluates did not bind IX. Purified patient inhibitors were eluted at low pH and contained detectable IgG1, IgG2 and IgG4 but not IgG3, IgA or IgM by radial immunodiffusion. On immunoradiometric assay, each patient's 125I-inhibitor bound to IX on the same solid phase inhibitor, indicating recognition of more than one epitope. Factor IX Ag was readily detected in these assays. The patients' inhibitors competed with binding of 125I-IX binding to each of 3 monoclonal antibodies. Each monoclonal antibody blocked 125I-IX binding to its own, insolubilized species. Similar results were obtained on an inhibitor plasma provided by H. Reisner (Chapel Hill, NC) which, unlike the present cases, contained a calcium-requiring antibody fraction (Briet E, et al Prog Clin Biol Res 150:123-139, 1984). Our patient's inhibitor was tested with two rabbit polyclonal fractions; the calcium-dependent fraction (epitopes in the light chain of IXa) and a specific heavy chain-binding fraction. The latter was from immunoaffinity purification of the non-calcium binding rabbit polyclonal fraction over an insolubilized synthetic peptide containing residues 256 through 269 of the IX sequence. Both fractions, in fluid phase, inhibited binding of 125I-IX to their own but not the other solid phase fraction. The patient's inhibitor did not block 125I-IX binding of the calcium-requiring fraction but did compete with the fraction prepared from the peptide column. These data suggest that the defect in our patient is a mutation between the Gla domain's 2nd or 3rd exons and the second growth factor-like region in the 5th exon." @default.
- W2992700530 created "2019-12-13" @default.
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- W2992700530 date "1987-01-01" @default.
- W2992700530 modified "2023-09-29" @default.
- W2992700530 title "ALLOANTIBODIES IN HEMOPHILIA B BINDING TO MULTIPLE FACTOR IX (IX) EPITOPES" @default.
- W2992700530 doi "https://doi.org/10.1055/s-0038-1644070" @default.
- W2992700530 hasPublicationYear "1987" @default.
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