Purification and functional analysis of Helicobacter pylori UreB protein fragment.
- Author:
Xiao-peng YUAN
1
;
Quan-ming ZHOU
;
Yang BAI
;
Jun YANG
;
Ying GUO
;
Wei-jun ZHANG
;
Zheng-xiang LIU
Author Information
- Publication Type:Journal Article
- MeSH: Amino Acid Sequence; Animals; Antibody Specificity; Bacterial Proteins; chemistry; Bacterial Vaccines; biosynthesis; chemistry; immunology; isolation & purification; Chromatography, High Pressure Liquid; Electrophoresis; Escherichia coli; genetics; Helicobacter pylori; genetics; immunology; Molecular Sequence Data; Peptide Fragments; biosynthesis; chemistry; immunology; isolation & purification; Rabbits; Urease; antagonists & inhibitors
- From: Journal of Southern Medical University 2007;27(7):959-962
- CountryChina
- Language:Chinese
-
Abstract:
OBJECTIVETo establish an effective method for purification of Helicobacter pylori UreB fragment and conduct functional analysis of the purified protein.
METHODSThe 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.
RESULTSThe 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.
CONCLUSIONThe UreB fragment with high purity and biological activity can be applied for further studies.
