Source:http://linkedlifedata.com/resource/pubmed/id/19433111
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-2
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pubmed:dateCreated |
2009-6-29
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pubmed:abstractText |
The core antigen of the hepatitis B virus (HBcAg) has been used widely as a diagnostic reagent for the identification of the viral infection. However, purification using the conventional sucrose density gradient ultracentrifugation is time consuming and costly. To overcome this, HBcAg particles displaying His-tag on their surface were constructed and produced in Escherichia coli. The recombinant His-tagged HBcAgs were purified using immobilized metal affinity chromatography. Transmission electron microscopy and enzyme-linked immunosorbent assay (ELISA) revealed that the displayed His-tag did not impair the formation of the core particles and the antigenicity of HBcAg.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1879-0984
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
160
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
125-31
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pubmed:meshHeading |
pubmed-meshheading:19433111-Chromatography, Affinity,
pubmed-meshheading:19433111-Escherichia coli,
pubmed-meshheading:19433111-Gene Expression,
pubmed-meshheading:19433111-Hepatitis B Core Antigens,
pubmed-meshheading:19433111-Microscopy, Electron, Transmission,
pubmed-meshheading:19433111-Recombinant Fusion Proteins,
pubmed-meshheading:19433111-Virosomes
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pubmed:year |
2009
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pubmed:articleTitle |
N-terminally His-tagged hepatitis B core antigens: construction, expression, purification and antigenicity.
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pubmed:affiliation |
Department of Microbiology, Universiti Putra Malaysia, Serdang, Selangor, Malaysia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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