Characterization of a monoclonal antibody that binds to an epitope on soluble bacterial peptidoglycan fragments.

@article{Merkel2001CharacterizationOA,
  title={Characterization of a monoclonal antibody that binds to an epitope on soluble bacterial peptidoglycan fragments.},
  author={Glenn J. Merkel and Barbara A. Scofield},
  journal={Clinical and diagnostic laboratory immunology},
  year={2001},
  volume={8 3},
  pages={
          647-51
        }
}
We employed an inhibition-type enzyme-linked immunosorbent assay (ELISA) to characterize a murine immunoglobulin M monoclonal antibody (MAb) that bound soluble macromolecular peptidoglycan (PG). With this ELISA, the MAb was capable of detecting soluble PG concentrations of less than 10 ng/ml. Enzymatic digestion of PG reduced binding by more than 100-fold, implying that the epitope recognized by this antibody depended on repeating subunits within the glycan backbone. Additionally, the MAb bound… CONTINUE READING
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