Please use this identifier to cite or link to this item:
Full metadata record
DC FieldValueLanguage
dc.contributor.authorSubramanian, Sarada-
dc.contributor.authorShree, A N Divya-
dc.description.abstractAlzheimer’s disease (AD) is a neurodegenerative disorder characterized by a progressive loss of cognitive function. Existing evidence indicates that abnormal processing and extracellular deposition of the longer form of the amyloid peptide Aβ(1-42), a proteolytic derivative of the amyloid precursor protein (APP), is a key step in the pathogenesis of AD. Active immunization with Aβ(1-42) has been shown to decrease brain Aβ deposition and improve cognitive performance in mouse models of AD. In the present study, we sought to express the synthetic gene encoding Aβ in Escherichia coli to enable rapid production of the antigen and its purification. The synthetic gene has been constructed from six oligonucleotides by employing overlapping PCR strategy and expressed in E. coli using the T7 promoter system. The recombinant peptide has been purified to homogeneity by a single step Ni+2 affinity chromatography. Enzyme-linked immunosorbent assay (ELISA) using polyclonal anti-Aβ(1-42) sera confirms that the corresponding linear B-cell epitopic sequences are available for immunorecognition in the recombinant peptide. This methodology enables rapid, continuous production and purification in bulk amounts of human Aβ sequence by employing bacterial expression systemen_US
dc.sourceIJBB Vol.44(2) [April 2007]en_US
dc.subjectAlzheimer’s diseaseen_US
dc.subjectAmyloid β peptideen_US
dc.subjectEscherichia colien_US
dc.subjectOverlapping PCRen_US
dc.subjectSynthetic geneen_US
dc.subjectPurification and characterizationen_US
dc.titleExpression, purification and characterization of a synthetic gene encoding human amyloid β (Aβ1-42) in Escherichia colien_US
Appears in Collections:IJBB Vol.44(2) [April 2007]

Files in This Item:
File Description SizeFormat 
IJBB 44(2) (2007) 71-75.pdf340.6 kBAdobe PDFView/Open

Items in NOPR are protected by copyright, with all rights reserved, unless otherwise indicated.