Purification and functional analysis of Helicobacter pylori UreB protein fragment / 南方医科大学学报
Journal of Southern Medical University
; (12): 959-962, 2007.
Article
in Zh
| WPRIM
| ID: wpr-337350
Responsible library:
WPRO
ABSTRACT
<p><b>OBJECTIVE</b>To establish an effective method for purification of Helicobacter pylori UreB fragment and conduct functional analysis of the purified protein.</p><p><b>METHODS</b>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.</p><p><b>RESULTS</b>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.</p><p><b>CONCLUSION</b>The UreB fragment with high purity and biological activity can be applied for further studies.</p>
Full text:
1
Index:
WPRIM
Main subject:
Peptide Fragments
/
Bacterial Proteins
/
Urease
/
Molecular Sequence Data
/
Bacterial Vaccines
/
Chemistry
/
Chromatography, High Pressure Liquid
/
Helicobacter pylori
/
Amino Acid Sequence
/
Electrophoresis
Limits:
Animals
Language:
Zh
Journal:
Journal of Southern Medical University
Year:
2007
Type:
Article