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Purification and characterization of the antimicrobial peptide, ostricacin

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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 aureus in vitro.

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Correspondence to Pak-Lam Yu.

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Yu, PL., Choudhury, S.D. & Ahrens, K. Purification and characterization of the antimicrobial peptide, ostricacin. Biotechnology Letters 23, 207–210 (2001). https://doi.org/10.1023/A:1005623806445

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  • DOI: https://doi.org/10.1023/A:1005623806445

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