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
em Zh
| WPRIM
| ID: wpr-337350
Biblioteca responsável:
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>
Texto completo:
1
Base de dados:
WPRIM
Assunto principal:
Fragmentos de Peptídeos
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Proteínas de Bactérias
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Urease
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Dados de Sequência Molecular
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Vacinas Bacterianas
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Química
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Cromatografia Líquida de Alta Pressão
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Helicobacter pylori
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Sequência de Aminoácidos
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Eletroforese
Limite:
Animals
Idioma:
Zh
Revista:
Journal of Southern Medical University
Ano de publicação:
2007
Tipo de documento:
Article