Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/116
Full metadata record
DC FieldValueLanguage
dc.contributor.authorZhu, Daling-
dc.contributor.authorLi, Aihua-
dc.contributor.authorWang, Jianguo-
dc.contributor.authorLi, Ming-
dc.contributor.authorCai, Taozhen-
dc.date.accessioned2008-02-20T11:17:49Z-
dc.date.available2008-02-20T11:17:49Z-
dc.date.issued2007-08-
dc.identifier.issn0301-1208-
dc.identifier.urihttp://hdl.handle.net/123456789/116-
dc.description204-208en_US
dc.description.abstractAerolysin is a toxin (protein in nature) secreted by the strains of Aeromonas spp. and plays an important role in the virulence of Aeromonas strains. It has also found several applications such as for detection of glycosylphosphatidylinositol (GPI)-anchored proteins etc. A. hydrophila is a ubiquitous Gram-negative bacterium which causes frequent harm to the aquaculture. To obtain a significant amount of recombinant aerolysin in the active form, in this study, we expressed the aerolysin in E. coli under the control of T7 RNase promoter. The coding region (AerA-W) of the aerA gene of A. hydrophila XS91-4-1, excluding partial coding region of the signal peptide was cloned into the vector pET32a and then transformed into E. coli bl21. After optimizing the expression conditions, the recombinant protein AerA-W was expressed in a soluble form and purified using His•Bind resin affinity chromatography. Recombinant aerolysin showed hemolytic activity in the agar diffusive hemolysis test. Western blot analysis demonstrated good antigenicity of the recombinant protein.en_US
dc.language.isoen_USen_US
dc.publisherCSIRen_US
dc.sourceIJBB Vol.44(4) [August 2007]en_US
dc.subjectAeromonas hydrophilen_US
dc.subjectCloningen_US
dc.subjectAerA geneen_US
dc.subjectProkaryotic expressionen_US
dc.subjectRecombinant protein AerA-Wen_US
dc.subjectHemolytic activityen_US
dc.titleCloning, expression and characterization of aerolysin from Aeromonas hydrophila in Escherichia colien_US
dc.typeArticleen_US
Appears in Collections:IJBB Vol.44(4) [August 2007]

Files in This Item:
File Description SizeFormat 
IJBB 44(4) (2007) 204-208.pdf271.95 kBAdobe PDFView/Open


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