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Journal of Southern Medical University ; (12): 959-962, 2007.
Article Dans Chinois | WPRIM | ID: wpr-337350

Résumé

<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>


Sujets)
Animaux , Lapins , Séquence d'acides aminés , Spécificité des anticorps , Protéines bactériennes , Chimie , Vaccins antibactériens , Chimie , Allergie et immunologie , Chromatographie en phase liquide à haute performance , Électrophorèse , Escherichia coli , Génétique , Helicobacter pylori , Génétique , Allergie et immunologie , Données de séquences moléculaires , Fragments peptidiques , Chimie , Allergie et immunologie , Urease
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