Purification and characterization of the antimicrobial peptide, ostricacin

@article{Yu2004PurificationAC,
  title={Purification and characterization of the antimicrobial peptide, ostricacin},
  author={Pak-Lam Yu and Santanu Deb Choudhury and Katja Ahrens},
  journal={Biotechnology Letters},
  year={2004},
  volume={23},
  pages={207-210}
}
An antimicrobial peptide, ostricacin-1, has been purified and characterized from ostrich leukocytes. The peptide has a mass of 4011 and contained 36 residues, including 3 intramolecular cystine disulfide bonds. Ostricacin-1 has a primary sequence homology to the β-defensin family and was active at 6.7 μg ml−1 against E. coli and Staphylocccus aureus in vitro.