Characterization of Cysteinylation and Trisulfide Bonds in a Recombinant Monoclonal Antibody.

@article{Kita2016CharacterizationOC,
  title={Characterization of Cysteinylation and Trisulfide Bonds in a Recombinant Monoclonal Antibody.},
  author={Adriana Z Kita and Gomathinayagam Ponniah and Christine Nowak and Hongcheng Liu},
  journal={Analytical chemistry},
  year={2016},
  volume={88 10},
  pages={
          5430-7
        }
}
A recombinant monoclonal antibody with trisulfide bonds and cysteinylation was thoroughly characterized in the current study. Trisulfide bonds and cysteinylation were first detected when the recombinant monoclonal antibody was analyzed by LC-MS to determine the molecular weights of the intact antibody and its F(ab')2 fragment generated from IdeS digestion. LC-MS analysis of nonreduced tryptic peptides indicated trisulfide bonds are associated with the interchain disulfide bonds of both A… CONTINUE READING
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References

Publications referenced by this paper.

ACS Paragon Plus Environment Analytical Chemistry 1 2 3 4 5

P. Pristatsky, S. L. Cohen, +3 authors J. Anal. Chem. Vlasak
  • 2009

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