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. 2003 Apr;12(4):734–747. doi: 10.1110/ps.0228503

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Figure 8. — Sensorgrams illustrating the binding hu3S193 scFv multimers to immobilized synthetic Le^y tetrasaccharide-BSA complex (2100 RU) at a constant flow rate of 5 μL/min with an injection volume of 35 μL. The surface was regenerated with 10 μL of 100 mM HCl after each cycle. (A) hu3S193 IgG (3.9, 7.9, 15.7nM), (B) hu3S193 +5 dimer (57.5, 115, 230nM), (C) hu3S193 +2 dimer (57.5, 115, 230nM), (D) V_H-0-V_L KR variant trimer (57.5, 115, 230nM), (E) reverse V_L-0-V_H trimer/tetramer (57.5, 115, 230nM), (F) hu3S193 (−1) trimer (57.5, 115, 230 nM). Monomeric forms (hu3S193 +15 and Fab) not shown, and dimeric forms (IgG and hu3S193 +5 and hu3S193 +2) exhibit monovalent binding with the surface whereas hu3S193 trimer and tetramer show multivalent binding as indicated by the dissociation rates.