Biotechnology Letters

, Volume 23, Issue 3, pp 207–210

Purification and characterization of the antimicrobial peptide, ostricacin

Article

DOI: 10.1023/A:1005623806445

Cite this article as:
Yu, PL., Choudhury, S.D. & Ahrens, K. Biotechnology Letters (2001) 23: 207. doi:10.1023/A:1005623806445

Abstract

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 aureusin vitro.

antimicrobial peptideβ-defensinostricacinostrich leukocytes

Copyright information

© Kluwer Academic Publishers 2001

Authors and Affiliations

  • Pak-Lam Yu
    • 1
  • Santanu Deb Choudhury
    • 1
  • Katja Ahrens
    • 1
  1. 1.Biotechnology Group, Institute of Technology and Engineering, College of SciencesMassey UniversityPalmerston NorthNew Zealand