Mass spectrometric determination of disulfide linkages in recombinant therapeutic proteins using online LC-MS with electron-transfer dissociation.

@article{Wu2009MassSD,
  title={Mass spectrometric determination of disulfide linkages in recombinant therapeutic proteins using online LC-MS with electron-transfer dissociation.},
  author={S Wu and Haitao Jiang and Qiaozhen Lu and Shujia Dai and William S. Hancock and Barry L. Karger},
  journal={Analytical chemistry},
  year={2009},
  volume={81 1},
  pages={112-22}
}
In the biotechnology industry, the generation of incorrectly folded recombinant proteins, either from an E.coli expression system or from an overexpressed CHO cell line (disulfide scrambling), is often a great concern as such incorrectly folded forms may not be completely removed in the final product. Thus, significant efforts have been devoted to map disulfide bonds to ensure drug quality. Similar to ECD, disulfide bond cleavages are preferred over peptide backbone fragmentation in ETD. Thus… CONTINUE READING
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