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大肠杆菌表达的rhIL-8的分离纯化

PURIFICATION AND IDENTIFICATION OF RECOMBINANT IL-8 OF EXPRESSION IN E,COLI

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【作者】 李卫党狄春辉白惠卿马大龙

【Author】 LI Weidang; DI Chunhui; BAI Huiqing; MA Dalong(Department of lmmunology.Beijing Medical University 100083)

【机构】 北京医科大学免疫学系

【摘要】 目的:探索人重组白细胞介素-8(rhIL-8)的分离纯化的路线。方法:用Sephacry1-S-200凝胶过滤和Qsepharosehighperformance,Qsepharosebigheadx两步连续阴离子交换层析纯化。结果:两种方法纯化的rhIL-8纯度分别达95.6%、98.6%。氨基酸组份分析推算值基本与理论值相符。纯化的rhIL-8对小鼠和人中性粒细胞具有明显的体内体外趋化作用。结论:本法为rhlL-8提供了快速高效的纯化路线。

【Abstract】 Objective:To study the purification and identification of recombinant IL-8.Methods:Two protocols were performed and compared.The first one purified rhlL-8 via passaging over Sephacryl-S-200 gel-filtration chromatography.The second one by two step ion-exchange chromatography.Results:The purified rhIL-8 were 95.6%and 98.6%homogeneity as analysis with SDS-PAGE,Respectively. and exhibited chemotaxis for neurophils in vitro and in vivo. Conclusion: The results provide rapidly and efficiently protocols for the purificatlon and identification of rhlL-8.

  • 【文献出处】 北京医科大学学报 ,JOURNAL OF BEIJING MEDICAL UNIVERSITY , 编辑部邮箱 ,1996年05期
  • 【分类号】R378.21
  • 【下载频次】181
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