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.