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Isolation and characterization of the recombinant human α-fetoprotein fragment corresponding to the C-terminal structural domain

机译:对应于C端结构域的重组人甲胎蛋白片段的分离和鉴定

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摘要

Alpha-fetoprotein (AFP) is the major human oncofetal protein. The receptor of AFP is expressed by cells of various tumors and is not produced by normal cells of the adult body. In an AFP molecule, the site of binding to its receptor is localized in the third domain. The conjugates of the natural AFP with a variety of cytostatics inhibited the growth of tumor cells in vivo and in vitro. The C-terminal fragment of AFP (amino acid residues 404-595 of the full-length protein) was cloned and expressed in cells of the Escherichia coli strain BL21(DE3). The yield of the protein was no less than 150 mg/l. A highly efficient method of its isolation and renaturation was developed so that the yield of the protein was no less than 50% with a purity of about 93%. The renatured third domain of AFP bound specifically to and penetrated into cells having the AFP receptor. The recombinant third domain of AFP can be used as a carrier for targeted drug delivery to tumor cells.
机译:甲胎蛋白(AFP)是人类主要的胎粪蛋白。 AFP的受体由各种肿瘤的细胞表达,而不是由成年人的正常细胞产生。在AFP分子中,与其受体结合的位点位于第三结构域中。天然AFP与多种细胞抑制剂的结合物在体内和体外抑制肿瘤细胞的生长。克隆AFP的C末端片段(全长蛋白质的氨基酸残基404-595)并在大肠杆菌菌株BL21(DE3)的细胞中表达。蛋白质的产量不低于150 mg / l。开发了一种高效的分离和复性方法,使蛋白质的收率不低于50%,纯度约为93%。变性的AFP的第三个结构域与具有AFP受体的细胞特异性结合并渗透。 AFP的重组第三结构域可以用作将药物靶向递送至肿瘤细胞的载体。

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