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“…Minor variations in pepscan profiles were also observed for MAb pairs PNF69C, PNF110A and G7C, JD312 that could reflect subtle differences in the spatial orientation of a MAb for a given epitope. Similar variations in reactivity have been reported in other studies [15,16]. Interestingly preliminary data from BIAcore analysis [35] using purified IgG paraprotein immobilised with a goat anti-mouse antibody, highlights differing affinity constants [PNF69C (4 )/10 7 per M), PNF110A (7.14)/ 10 7 per M), G7C (2.70)/10 8 per M), JD312 (2.86)/10 8 per M), TM15 (2 )/10 8 per M)] that might reflect subtle variations in Mab Á/epitope interactions.…”
Section: Discussionsupporting
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“…Minor variations in pepscan profiles were also observed for MAb pairs PNF69C, PNF110A and G7C, JD312 that could reflect subtle differences in the spatial orientation of a MAb for a given epitope. Similar variations in reactivity have been reported in other studies [15,16]. Interestingly preliminary data from BIAcore analysis [35] using purified IgG paraprotein immobilised with a goat anti-mouse antibody, highlights differing affinity constants [PNF69C (4 )/10 7 per M), PNF110A (7.14)/ 10 7 per M), G7C (2.70)/10 8 per M), JD312 (2.86)/10 8 per M), TM15 (2 )/10 8 per M)] that might reflect subtle variations in Mab Á/epitope interactions.…”
Section: Discussionsupporting
“…Epitope mapping of MAbs G7C and JD312 identified the core peptide sequence 290-KPREE-294 that was present in all four IgG subclasses ( Table 2) and was consistent with the pan-IgG reactivity exhibited by these antibodies in previous studies [15,16]. The latter also serve to demonstrate that the binding of MAbs G7C and JD312 to IgG is not rendered inaccessible by oligosaccharide moieties linked via asparagine 297 [32] or influenced by leucine 291 .…”
Section: Discussionsupporting
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