...
首页> 外文期刊>Applied Biochemistry and Microbiology >Examination of bovine lactoferrin binding to bifidobacteria
【24h】

Examination of bovine lactoferrin binding to bifidobacteria

机译:牛乳铁蛋白与双歧杆菌结合的检查

获取原文
获取原文并翻译 | 示例
   

获取外文期刊封面封底 >>

       

摘要

In the present study, lactoferrin binding to bifidobacteria and detection of lactoferrin-binding protein in membrane fractions of several bifidobacteria have been demonstrated. This is the first report showing the binding of bovine lactoferrin to four Bifidobacterium spp. (B. infantis, B. breve, B. bifidum, and B. longum) incubated with biotinylated lactoferrin and fluorescein-conjugated avidin and observed under an inverted confocal laser scanning microscope. Fluorescence staining showed lactoferrin binding at the pole of the bacterial cells. A lactoferrin-binding protein with a molecular weight of approximately 67 kDa was also detected in the membrane fraction of Bifidobacterium spp. by far-western blotting technique using biotinylated lactoferrin and horseradish peroxidase-conjugated streptavidin. Based on the results of this and previously reported studies, we suggest that binding of lactoferrin to Bifidobacterium longum is strain dependent. [PUBLICATION ABSTRACT]
机译:在本研究中,已证明乳铁蛋白与双歧杆菌结合以及在几种双歧杆菌的膜级分中检测乳铁蛋白结合蛋白。这是首次报道牛乳铁蛋白与四种双歧杆菌属的结合。与生物素化的乳铁蛋白和荧光素缀合的抗生物素蛋白孵育的细菌(婴儿双歧杆菌,短双歧杆菌,双歧双歧杆菌和长双歧杆菌)和在倒置共聚焦激光扫描显微镜下观察。荧光染色显示乳铁蛋白在细菌细胞的极点结合。在双歧杆菌属的膜级分中也检测到分子量约为67 kDa的乳铁蛋白结合蛋白。通过使用生物素化的乳铁蛋白和辣根过氧化物酶结合的抗生蛋白链菌素的远古印迹技术。根据此研究结果和以前的研究结果,我们建议乳铁蛋白与长双歧杆菌的结合是菌株依赖性的。 [出版物摘要]

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号