New antibacterial peptide derived from bovine hemoglobin
Peptic digestion of bovine hemoglobin at low degree of hydrolysis yields an intermediate peptide fraction exhibiting antibacterial activity against Micrococcus luteus A270, Listeria innocua, Escherichia coli and Salmonella enteritidis after separation by reversed-phase HPLC. From this fraction a pur...
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Veröffentlicht in: | Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2005-05, Vol.26 (5), p.713-719 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Peptic digestion of bovine hemoglobin at low degree of hydrolysis yields an intermediate peptide fraction exhibiting antibacterial activity against
Micrococcus luteus A270,
Listeria innocua,
Escherichia coli and
Salmonella enteritidis after separation by reversed-phase HPLC. From this fraction a pure peptide was isolated and analyzed by matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) and electrospray ionization tandem mass spectrometry (ESI-MS/MS). This peptide correspond to the 107–136 fragment of the α chain of bovine hemoglobin. The minimum inhibitory concentrations (MIC) towards the four strains and its hemolytic activity towards bovine erythrocytes were determined. A MIC of 38
μM was reported against
L. innocua and 76
μM for other various bacterial species. This peptide had no hemolytic activity up to 380
μM concentration. |
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ISSN: | 0196-9781 1873-5169 |
DOI: | 10.1016/j.peptides.2004.12.008 |