Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2009-6-29
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1879-0984
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
160
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
125-31
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
N-terminally His-tagged hepatitis B core antigens: construction, expression, purification and antigenicity.
pubmed:affiliation
Department of Microbiology, Universiti Putra Malaysia, Serdang, Selangor, Malaysia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't