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在动物乳中生产人乳铁蛋白。

Production of human lactoferrin in animal milk.

机构信息

Institute of Gene Biology, Russian Academy of Sciences, 119334, Vavilova str, 34/5, Moscow, Russia.

出版信息

Biochem Cell Biol. 2012 Jun;90(3):513-9. doi: 10.1139/o11-088. Epub 2012 Feb 23.

DOI:10.1139/o11-088
PMID:22360490
Abstract

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.

摘要

俄罗斯和白俄罗斯科学家合作创建了含有人类乳铁蛋白(hLf)基因的遗传构建体。利用这些构建体,培育出了转基因小鼠(其乳汁中 hLf 的浓度最高可达 160 g/L),也培育出了转基因山羊(其乳汁中 hLf 的浓度最高可达 10 g/L)。还培育出了能在乳汁中产生 hLf 的实验性奶山羊,重组 hLf 在物理和化学性质上与天然蛋白完全相同。这些性质包括电泳迁移率、等电点、多克隆和单克隆抗体的识别、圆二色性光谱、与天然配体(DNA、脂多糖和肝素)的相互作用、铁离子结合、7 个末端氨基酸序列以及其生物活性。后者通过微球菌原生质体的凝集、对大肠杆菌和李斯特菌的杀菌活性以及对白色念珠菌的杀菌活性来评估。我们还证明了与 Lf 联合使用时抗生素活性显著增强。

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Study of pH and Thermodynamic Parameters via Circular Dichroism Spectroscopy of a Recombinant Human Lactoferrin.通过圆二色光谱法对重组人乳铁蛋白的pH值和热力学参数进行研究。
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