Froidevaux R, Krier F, Nedjar-Arroume N, Vercaigne-Marko D, Kosciarz E, Ruckebusch C, Dhulster P, Guillochon D
Laboratoire de Technologie des Substances Naturelles, Institut Universitaire de Technologie, Département Génie Biologique, Université des Sciences et Technologie de Lille, PO Box 179, 59653 Villeneuve d'Ascq Cedex, France.
FEBS Lett. 2001 Feb 23;491(1-2):159-63. doi: 10.1016/s0014-5793(01)02171-8.
Peptic digestion of bovine hemoglobin yields a fragment with antibacterial activity. This peptide was purified to homogeneity by a two-step procedure including anion exchange chromatography and preparative reversed-phase HPLC. Mass determination and fragmentation indicated that this peptide corresponded to the 1-23 fragment of the alpha chain of hemoglobin. The minimum inhibitory concentration and mode of action of this peptide towards Micrococcus luteus strain A270 were determined. Hemolytic assay, interaction with liposomes, and study of its structure in solution were also performed.
牛血红蛋白的胃蛋白酶消化产生一种具有抗菌活性的片段。该肽通过两步法纯化至同质，包括阴离子交换色谱和制备型反相高效液相色谱。质量测定和片段分析表明，该肽对应于血红蛋白α链的1-23片段。测定了该肽对藤黄微球菌A270菌株的最小抑菌浓度和作用方式。还进行了溶血试验、与脂质体的相互作用以及其在溶液中的结构研究。
