In vitro enzymatic biotinylation of recombinant fab fragments through a peptide acceptor tail.

@article{Saviranta1998InVE,
  title={In vitro enzymatic biotinylation of recombinant fab fragments through a peptide acceptor tail.},
  author={Petri Saviranta and Tapio E Haavisto and Pekka Rappu and Matti Karp and Timo L{\"o}vgren},
  journal={Bioconjugate chemistry},
  year={1998},
  volume={9 6},
  pages={725-35}
}
We describe the site-specific enzymatic biotinylation of recombinant anti-estradiol Fab fragments through a 13 amino acid acceptor peptide translationally fused to the C-terminus of the Fd chain. The Fab-peptide fusion proteins were secreted to the periplasm of Escherichia coli, purified, and biotinylated in vitro using biotin ligase, biotin, and ATP. The E… CONTINUE READING