Please use this identifier to cite or link to this item: http://ir.swu.ac.th/jspui/handle/123456789/14380
Full metadata record
DC FieldValueLanguage
dc.contributor.authorKhawsak P.
dc.contributor.authorKanjanavas P.
dc.contributor.authorKiatsomchai P.
dc.contributor.authorChansiri K.
dc.date.accessioned2021-04-05T03:34:29Z-
dc.date.available2021-04-05T03:34:29Z-
dc.date.issued2012
dc.identifier.issn9320113
dc.identifier.other2-s2.0-84857059728
dc.identifier.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-84857059728&doi=10.1007%2fs00436-011-2532-z&partnerID=40&md5=221f7a69f0ec7c272a5ce7d65ed12488
dc.identifier.urihttp://ir.swu.ac.th/jspui/handle/123456789/14380-
dc.description.abstractThe Cu/Zn superoxide dismutase gene from Wuchereria bancrofti (Cu/Zn WbSOD) was isolated by PCR using degeneracy primers. The complete Cu/Zn WbSOD consisted of 1,032 nucleotides containing 4 exons (477 nucleotides) and 3 introns. The molecular phylogenetic analysis of the Cu/Zn WbSOD gene in comparison with those from other organisms revealed that the gene was classified in the same clade to those of filarial Brugia malayi and Brugia pahangi (bootstrap value at 90). The nucleotide and deduced amino acid sequences of Cu/Zn WbSOD exhibited the similarity to those of intracellular Cu/Zn SOD of B. malayi and B. pahangi. The amino acid comparison of Cu/Zn WbSOD to others revealed that the binding sites and active sites were conserved. The expression of this gene yielded 16.366 kDa in size. After Ni-IDA column purification, the enzyme showed specific activity of 8.5 U/mg and 42.1% yield. The enzyme activity was inhibited when 6 mM KCN was added. © Springer-Verlag 2011.
dc.subjectcopper zinc superoxide dismutase
dc.subjectnucleotide
dc.subjectpotassium cyanide
dc.subjectamino acid sequence
dc.subjectarticle
dc.subjectbinding site
dc.subjectbootstrapping
dc.subjectBrugia malayi
dc.subjectBrugia pahangi
dc.subjectcladistics
dc.subjectcontrolled study
dc.subjectenzyme active site
dc.subjectenzyme activity
dc.subjectenzyme analysis
dc.subjectenzyme isolation
dc.subjectexon
dc.subjectFilaria
dc.subjectgene
dc.subjectgene expression
dc.subjecthuman
dc.subjecthuman tissue
dc.subjectintron
dc.subjectmolecular phylogeny
dc.subjectnonhuman
dc.subjectnucleotide sequence
dc.subjectpolymerase chain reaction
dc.subjectpriority journal
dc.subjectprotein expression
dc.subjectWuchereria bancrofti
dc.subjectAnimals
dc.subjectBinding Sites
dc.subjectCatalytic Domain
dc.subjectCloning, Molecular
dc.subjectCluster Analysis
dc.subjectConserved Sequence
dc.subjectDNA Primers
dc.subjectDNA, Helminth
dc.subjectEnzyme Inhibitors
dc.subjectExons
dc.subjectGene Expression
dc.subjectIntrons
dc.subjectMolecular Sequence Data
dc.subjectMolecular Weight
dc.subjectPhylogeny
dc.subjectPolymerase Chain Reaction
dc.subjectPotassium Cyanide
dc.subjectRecombinant Proteins
dc.subjectSequence Analysis, DNA
dc.subjectSequence Homology, Amino Acid
dc.subjectSuperoxide Dismutase
dc.subjectWuchereria bancrofti
dc.subjectBrugia malayi
dc.subjectBrugia pahangi
dc.subjectWuchereria bancrofti
dc.titleExpression and characterization of Cu/Zn superoxide dismutase from Wuchereria bancrofti
dc.typeArticle
dc.rights.holderScopus
dc.identifier.bibliograpycitationParasitology Research. Vol 110, No.2 (2012), p.629-636
dc.identifier.doi10.1007/s00436-011-2532-z
Appears in Collections:Scopus 1983-2021

Files in This Item:
There are no files associated with this item.


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