Liu et al. (20step one0a) determined the relative susceptibility of all of the disulfide bonds of a human IgG1 to reduction, and found that inter-chain disulfide bridges between the heavy chain (HC) and the light chain (LC) were the most labile, followed by the two HC–HC disulfide bridges of the hinge (the most N-terminal of which was more susceptible than the other). L, CL, VH, and CH1 domains, and finally the CHstep 3 domain, which was most stable to reduction ( Liu et al., 2010a ). They also determined that the LC–HC inter-chain bonds of IgG1? were more labile than those of IgG1? ( Liu et al., 2010a ), a result similar to that found by Montano and Morrison (2002) with IgG2? vs IgG2?. The C-terminus of C? ends in the Cys residue that bridges to the HC, but with C?, the disulfide bridging Cys residue is followed by a Ser residue, which is the C-terminal residue of that chain ( Liu et al., 2011a ). The presence of that Ser residue (or even if changed to an Ala residue) was found to be the cause for the increase in lability of the IgG1? HC–LC disulfide bridge. Deletion of that C-terminal residue increased the stability of the IgG1? Continue reading “Of the intra-strings disulfide bonds, those in brand new C”
