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A Study of Recombinant Human Lactoferrin Secreted in Milk of Transgenic Mice

机译:转基因小鼠乳汁中分泌的重组人乳铁蛋白的研究

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In this study, the properties of recombinant human lactoferrin isolated from milk of transgenic mice and natural human lactoferrin obtained isolated from breast milk were compared. Identity of both proteins was confirmed using by electrophoretic, immunological, and chromatographic methods. The lactoferrin from milk of transgenic mice exhibited the properties characteristic of human lactoferrin: it effectively chelated iron ions and binds to DNA, heparin, and bacterial lipopolysac-charide. Both proteins displayed identical bactericidal and fungicidal activities. The data obtained in this study allow the created genetic constructs to be used for obtaining producers of human lactoferrin on the basis of farm animals.
机译:在这项研究中,比较了从转基因小鼠的乳汁中分离的重组人乳铁蛋白和从母乳中分离的天然人乳铁蛋白的特性。通过电泳,免疫学和色谱法确认两种蛋白质的身份。转基因小鼠乳汁中的乳铁蛋白表现出人乳铁蛋白的特性:它有效螯合铁离子,并与DNA,肝素和细菌脂多糖结合。两种蛋白质均显示出相同的杀菌和杀真菌活性。在这项研究中获得的数据允许所创建的遗传构建体用于在农场动物的基础上获得人乳铁蛋白的生产者。

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