Biotin-protein bond: instability and structural modification to provide stability for in vivo applications.

@article{Mock2008BiotinproteinBI,
  title={Biotin-protein bond: instability and structural modification to provide stability for in vivo applications.},
  author={Donald M. Mock and Anna Bogusiewicz},
  journal={Methods in molecular biology},
  year={2008},
  volume={418},
  pages={
          209-20
        }
}
Biotinylation of proteins is a powerful tool for investigating biological phenomenon, both in vitro and in vivo. Biotinylating reagents that form covalent bonds with several types of amino acid residues are commercially available. However, most, if not all, of these commercially available biotinylating agents produce biotin-protein bonds that are susceptible to cleavage in human plasma. Here, we describe the use of immunoglobulin G as a model protein for evaluation of biotin-protein bond… CONTINUE READING

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