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. Author manuscript; available in PMC: 2017 Oct 6.
Published in final edited form as: Anal Methods. 2016 Jul 27;8(31):6046–6055. doi: 10.1039/C6AY01248E

Figure 2.

Figure 2

(A) Structure of a typical human IgG3 antibody showing the disulfide bond pattern. There are a total of 50 Cys residues and 25 disulfide bonds (–S–S–). The red parts are the variable (V) regions and the black parts are the constant (C) regions. H and L indicate the heavy and light chains, respectively; VL and CL are domains of the light chain; VH, CH1, CH2, and CH3 are domains of the heavy chain. The hinge region has a 15-residue segment that is repeated three times. (B) Expected tryptic dipeptides from human IgG3 constant region.