Please use this identifier to cite or link to this item: http://ir.swu.ac.th/jspui/handle/123456789/14380
Title: Expression and characterization of Cu/Zn superoxide dismutase from Wuchereria bancrofti
Authors: Khawsak P.
Kanjanavas P.
Kiatsomchai P.
Chansiri K.
Keywords: copper zinc superoxide dismutase
nucleotide
potassium cyanide
amino acid sequence
article
binding site
bootstrapping
Brugia malayi
Brugia pahangi
cladistics
controlled study
enzyme active site
enzyme activity
enzyme analysis
enzyme isolation
exon
Filaria
gene
gene expression
human
human tissue
intron
molecular phylogeny
nonhuman
nucleotide sequence
polymerase chain reaction
priority journal
protein expression
Wuchereria bancrofti
Animals
Binding Sites
Catalytic Domain
Cloning, Molecular
Cluster Analysis
Conserved Sequence
DNA Primers
DNA, Helminth
Enzyme Inhibitors
Exons
Gene Expression
Introns
Molecular Sequence Data
Molecular Weight
Phylogeny
Polymerase Chain Reaction
Potassium Cyanide
Recombinant Proteins
Sequence Analysis, DNA
Sequence Homology, Amino Acid
Superoxide Dismutase
Wuchereria bancrofti
Brugia malayi
Brugia pahangi
Wuchereria bancrofti
Issue Date: 2012
Abstract: The 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.
URI: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84857059728&doi=10.1007%2fs00436-011-2532-z&partnerID=40&md5=221f7a69f0ec7c272a5ce7d65ed12488
http://ir.swu.ac.th/jspui/handle/123456789/14380
ISSN: 9320113
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.