Purification and characterization of the antimicrobial peptide, ostricacin

Authors
Yu, PL Choudhury, SD Ahrens, K
Citation
Pl. Yu et al., Purification and characterization of the antimicrobial peptide, ostricacin, BIOTECH LET, 23(3), 2001, pp. 207-210
Citations number
13
Categorie Soggetti
Biotecnology & Applied Microbiology",Microbiology
Journal title
BIOTECHNOLOGY LETTERS
ISSN journal
01415492 → ACNP
Volume
23
Issue
3
Year of publication
2001
Pages
207 - 210
Database
ISI
SICI code
0141-5492(200102)23:3<207:PACOTA>2.0.ZU;2-#
Abstract
An antimicrobial peptide, ostricacin-1, has been purified and characterized from ostrich leukocytes. The peptide has a mass of 4011 and contained 36 r esidues, including 3 intramolecular cystine disulfide bonds. Ostricacin-1 h as a primary sequence homology to the beta -defensin family and was active at 6.7 mug ml(-1) against E. coli and Staphylocccus aureus in vitro.