Ranking the susceptibility of disulfide bonds in human IgG1 antibodies by reduction, differential alkylation, and LC-MS analysis.

@article{Liu2010RankingTS,
  title={Ranking the susceptibility of disulfide bonds in human IgG1 antibodies by reduction, differential alkylation, and LC-MS analysis.},
  author={Hongcheng Liu and Chris M. Chumsae and Georgeen S Gaza-Bulseco and Karen Hurkmans and Czeslaw H Radziejewski},
  journal={Analytical chemistry},
  year={2010},
  volume={82 12},
  pages={5219-26}
}
One of the basic structural features of human IgG1 is the arrangement of the disulfide bond structure, 4 inter chain disulfide bonds in the hinge region and 12 intra chain disulfide bonds associated with twelve individual domains. Disulfide bond structure is critical for the structure, stability, and biological functions of IgG molecules. It has been known that inter chain disulfide bonds are more susceptible to reduction than intra chain disulfide bonds. However, a complete ranking of the… CONTINUE READING

From This Paper

Topics from this paper.
22 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 22 extracted citations

Similar Papers

Loading similar papers…