[Purification and functional analysis of Helicobacter pylori UreB protein fragment].

To establish an effective method for purification of Helicobacter pylori UreB fragment and conduct functional analysis of the purified protein.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.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.The UreB fragment with high purity and biological activity can be applied for further studies.