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Production of human lactoferrin in animal milk

机译:在动物乳中生产人乳铁蛋白

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摘要

Genetic constructs containing the human lactoferrin (hLf) gene were created within a joint program of Russian and Belorussian scientists. Using these constructs, transgenic mice were bred (the maximum hLf concentration in their milk was 160 g/L), and transgenic goats were also generated (up to 10 g/L hLf in their milk). Experimental goatherds that produced hLf in their milk were also bred, and the recombinant hLf was found to be identical to the natural protein in its physical and chemical properties. These properties included electrophoretic mobility, isoelectric point, recognition by polyclonal and monoclonal antibodies, circular dichroic spectra, interaction with natural ligands (DNA, lipopolysaccharides, and heparin), the binding of iron ions, the sequence of the 7 terminal amino acids, and its biological activity. The latter was assessed by the agglutination of Micrococcus luteus protoplasts, bactericidal activity against Escherichia coli and Listeria monocytogenes, and fungicidal activity against Candida albicans. We also demonstrated a significant increase in the activity of antibiotics when used in combination with Lf.
机译:在俄罗斯和白俄罗斯科学家的共同计划下,创建了包含人乳铁蛋白(hLf)基因的遗传构建体。使用这些构建体,饲养了转基因小鼠(牛奶中的最大hLf浓度为160 g / L),还产生了转基因山羊(牛奶中的hLf高达10 g / L)。还繁殖了在牛奶中产生hLf的实验性山羊奶,发现重组hLf的物理和化学性质与天然蛋白相同。这些特性包括电泳迁移率,等电点,多克隆和单克隆抗体识别,二向色光谱,与天然配体(DNA,脂多糖和肝素)的相互作用,铁离子的结合,7个末端氨基酸的序列及其生物活性。后者通过黄褐微球菌原生质体的凝集,对大肠杆菌和单核细胞增生李斯特氏菌的杀菌活性以及对白色念珠菌的杀真菌活性进行评估。当与Lf组合使用时,我们还证明了抗生素活性的显着提高。

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