Antibacterial peptides of bovine lactoferrin: purification and characterization.

@article{Dionysius1997AntibacterialPO,
  title={Antibacterial peptides of bovine lactoferrin: purification and characterization.},
  author={D A Dionysius and J M Milne},
  journal={Journal of dairy science},
  year={1997},
  volume={80 4},
  pages={667-74}
}
Three peptides with antibacterial activity toward enterotoxigenic Escherichia coli have been purified from a pepsin digest of bovine lactoferrin. All peptides were cationic and originated from the N-terminus of the molecule in a region where a bactericidal peptide, lactoferricin B, had been previously identified. The most potent peptide, peptide I, was almost identical to lactoferricin B; the sequence corresponded to residues 17 to 42, and the molecular mass was 3195 as determined by mass… CONTINUE READING

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