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Updated: Jul 13, 2026

One-step Negative Chromatographic Purification of Helicobacter pylori Neutrophil-activating Protein Overexpressed in Escherichia coli in Batch Mode
Published on: June 18, 2016
[Purification and functional analysis of Helicobacter pylori UreB protein fragment]
Xiao-peng Yuan1, Quan-ming Zhou, Yang Bai
1Department of Clinical Laboratory, Zhujiang Hospital, Southern Medical University, Guangzhou 510282, China. yuanxp2001@yahoo.com.cn
Objective:
To establish an effective method for purification of Helicobacter pylori UreB fragment and conduct functional analysis of the purified protein.
Methods:
The protein fragment expression was induced by IPTG and the expressed protein was purified through affinity chromatography and ion-exchange chromatography. The purity of the fragment was determined by high-performance liquid chromatography (HPLC), and the specific biological activity of the purified fragment was assayed by urease activity inhibition test.
Results:
The protein fragment was highly expressed in E. coli with a purity over 91%. The protein fragment showed highly specific biological activity and the specific antibody induced by this fragment in rabbits could inhibit the activity of urease in a dose-dependent manner.
Conclusion:
The UreB fragment with high purity and biological activity can be applied for further studies.
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