猪白细胞介素-4重组蛋白的纯化及其生物学特性分析

畜牧兽医学报 ›› 2007, Vol. 38 ›› Issue (10): 1072-1076.doi:

猪白细胞介素-4重组蛋白的纯化及其生物学特性分析

陈国华;景志忠;窦永喜;蒙学莲;张巧颖;宋世斌

中国农业科学院兰州兽医研究所，家畜疫病病原生物学国家重点实验室/甘肃省动物寄生虫病重点实验室，兰州 730046

收稿日期:1900-01-01 修回日期:1900-01-01 出版日期:2007-10-25 发布日期:2007-10-25

Purification and Bioactivity Analysis of Porcine IL-4 Recombinant Protein

CHEN Guo-hua;JING Zhi-zhong;DOU Yong-xi;MENG Xue-lian;ZHANG Qiao-ying;SONG Shi-bin

Key Laboratory of Veterinary Parasitology of Gansu Province/State Key Laboratory of Veterinary Etiological Biology，Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou 730046,China

Received:1900-01-01 Revised:1900-01-01 Online:2007-10-25 Published:2007-10-25

摘要/Abstract

摘要： 用已构建好的重组表达载体pGEX-4T-IL-4转染E-coli，在最适条件下诱导表达，表达产物经SDS-PAGE分析，表达出38 ku的融合蛋白，表达量占菌体总蛋白的25%，表达产物主要以包涵体的形式存在;对表达产物经变性、复性及初步纯化后再结合饱和硫酸铵沉淀和SephadexG100凝胶层析柱进一步纯化，所得蛋白的纯度约在90%以上。在体外利用MTT法检测其生物学特性，结果表明其具有较好的生物学活性，本试验为获得猪IL-4重组蛋白奠定了基础。

Abstract: The recombinant expression vector pGEX-IL-4 was induced by IPTG in optimal conditions in E.coli.SDS-PAGE analysis showed that the expressed fusion protein with a molecular weight of 38 ku existed in the inclusion body. The fusion protein, which was of 25% in total bacterial proteins, was denatured, renatured, and purified with saturated ammonium sulfate precipitation and Sephadex-G100 with the purity of above 90%. MTT analysis indicated that purified protein has good bioactivity, which has laid a foundation for the production and development of recombinant protein of porcine IL-4.

陈国华;景志忠;窦永喜;蒙学莲;张巧颖;宋世斌. 猪白细胞介素-4重组蛋白的纯化及其生物学特性分析[J]. 畜牧兽医学报, 2007, 38(10): 1072-1076.

CHEN Guo-hua;JING Zhi-zhong;DOU Yong-xi;MENG Xue-lian;ZHANG Qiao-ying;SONG Shi-bin. Purification and Bioactivity Analysis of Porcine IL-4 Recombinant Protein[J]. ACTA VETERINARIA ET ZOOTECHNICA SINICA, 2007, 38(10): 1072-1076.

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