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
Dans Chinois
| WPRIM
| ID: wpr-337350
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>
Texte intégral:
Disponible
Indice:
WPRIM (Pacifique occidental)
Sujet Principal:
Fragments peptidiques
/
Protéines bactériennes
/
Urease
/
Données de séquences moléculaires
/
Vaccins antibactériens
/
Chimie
/
Chromatographie en phase liquide à haute performance
/
Helicobacter pylori
/
Séquence d'acides aminés
/
Électrophorèse
Limites du sujet:
Animaux
langue:
Chinois
Texte intégral:
Journal of Southern Medical University
Année:
2007
Type:
Article
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