Preparation and characterization of disulfide stabilized Fv fragment antibody against N-terminal fragment of human lipopolysaccharide binding protein

邹佳; 葛晓冬; 杨艳丽; 刘友生

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Preparation and characterization of disulfide stabilized Fv fragment antibody against N-terminal fragment of human lipopolysaccharide binding protein

更新时间：2026-01-09

- Preparation and characterization of disulfide stabilized Fv fragment antibody against N-terminal fragment of human lipopolysaccharide binding protein
- Journal of Army Medical University Vol. 30, Issue 14, Pages: 1308-1311(2008)
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  CLC： R392-33;R392.11;R967
- Published：2008
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邹佳,葛晓冬,杨艳丽,刘友生.抗人氨基末端脂多糖结合蛋白二硫键稳定性Fv抗体的制备及生物学活性的初步研究[J].陆军军医大学学报(原第三军医大学学报),2008,30(14):1308-1311.

　ZOU Jia,GE Xiao-dong,YANG Yan-li,LIU You-sheng.Preparation and characterization of disulfide stabilized Fv fragment antibody against N-terminal fragment of human lipopolysaccharide binding protein[J].J Amry Med Univ (J Third Mil Med Univ),2008,30(14):1308-1311.
邹佳,葛晓冬,杨艳丽,刘友生.抗人氨基末端脂多糖结合蛋白二硫键稳定性Fv抗体的制备及生物学活性的初步研究[J].陆军军医大学学报(原第三军医大学学报),2008,30(14):1308-1311. DOI：

　ZOU Jia,GE Xiao-dong,YANG Yan-li,LIU You-sheng.Preparation and characterization of disulfide stabilized Fv fragment antibody against N-terminal fragment of human lipopolysaccharide binding protein[J].J Amry Med Univ (J Third Mil Med Univ),2008,30(14):1308-1311. DOI：

摘要

目的制备抗人氨基末端脂多糖结合蛋白（N-terminal fragment of human lipopolysaccharide binding protein，NH-LBP）的二硫键稳定性Fv抗体(disulfide stabilized Fv fragment，dsFv)，并初步测定其生物学活性。方法将含有dsFvV

与dsFvV

包涵体蛋白经复性、折叠和纯化，获得完整的dsFv抗体。通过ELISA、TNF-α分泌等方法，初步测定dsFv抗体在体内外的生物学活性。结果获得dsFv抗体蛋白约2.1 mg，dsFv与NH-LBP有较好的结合能力，并在动物体内减轻了LPS所诱导的炎症反应，发挥了一定的保护活性。结论通过分别表达V

和V

片段，再制备dsFv抗体是可行的，dsFv能部分抑制LBP的生物学功能。

Abstract

Objective To obtain the disulfide stabilized Fv fragment (dsFv) against N-terminal fragment of human lip polysaccharide binding protein (NH-LBP) and to identify its biological vitality. Methods The disulfide stabilized Fv fragment antibody (dsFv) was obtained after the inclusion bodies of dsFvV

and dsFvV

had been refolded and purified. Then the characteristics of dsFv were determined in vitro by ELISA and by detecting the secretion of tumor necrosis factor alpha (TNF-α) in rats. Results There was 2.1 mg protein of dsFv obtained. dsFv had go

od combination with NH-LBP and could restrain inflammatory reaction caused by lip polysaccharide (LPS) in vivo. Conclusion It is feasible to get dsFv against NH-LBP by respective expression of V

and V

. The partial inhibition of the biological function of LBP by dsFv is a new way to restrain the over-inflammatory reaction in vivo.

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