PMID: 9540819Apr 16, 1998Paper

Identification of a distinct antibacterial domain within the N-lobe of ovotransferrin

Biochimica Et Biophysica Acta
H R IbrahimT Aoki

Abstract

We have evaluated the bactericidal activity of hen ovotransferrin (OTf), which was found to operate regardless of its iron-deprivation properties, with the objective of isolating the bactericidal domain. The amino-terminal half-molecule (N-lobe, residues 1-332) of OTf, isolated by trypsin-nicking, retained the bactericidal activity independently of iron-deprivation, but not the carboxyl-terminal half-molecule (C-lobe, residue 342-686), suggesting the presence of a bactericidal domain within the N-lobe of the molecule. Specific cleavage at the aspartyl residues of OTf, by diluted-acid procedure, yielded fairly large peptides, whereas proteolysis for 150 min produced the strongest bactericidal peptides mixture. The bactericidal domain was purified from the active hydrolysate by gel filtration and reversed-phase HPLC and showed activity against S. aureus as well as E. coli K-12. Electrophoretic analysis on tricine-SDS-PAGE revealed a bactericidal peptide with an average M(r) of 9900 Da under non-reducing conditions. In combination with the specificity of cleavage (Asp-X) and the molecular mass, its N-terminal microsequencing corresponded to a cationic peptide consisting of 92 residues located within the 109-200 sequence of the N-l...Continue Reading

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Citations

Aug 24, 2012·Amino Acids·Aleksandra ZambrowiczTadeusz Trziszka
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