New antibacterial peptide derived from bovine hemoglobin

被引：97

作者：

Daoud, R

Dubois, V

Bors-Dodita, L

Nedjar-Arroume, N

Krier, F

Chihib, NE

Mary, P

Kouach, M

Briand, G

Guillochon, D

机构：

[1] IUT A Lille 1, Lab Technol Subst Nat, F-59653 Villeneuve Dascq, France

[2] Univ Lille 2, Fac Med H Warembourg, Lab Applicat Spectrometrie Masse, Serv Commun Physicochim, F-59800 Lille, France

来源：

PEPTIDES | 2005年 / 26卷 / 05期

关键词：

antibacterial peptide; bovine hemoglobin; pepsin; active peptide; hydrolysate;

D O I：

10.1016/j.peptides.2004.12.008

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

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 01 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 mu M was reported against L innocua and 76 mu M for other various bacterial species. This peptide had no hemolytic activity up to 380 mu M concentration. (c) 2004 Published by Elsevier Inc.

引用

页码：713 / 719

页数：7

共 22 条

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DETERMINATION OF THE DEGREE OF HYDROLYSIS OF FOOD PROTEIN HYDROLYSATES BY TRINITROBENZENESULFONIC ACID [J].