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https://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://ir.swu.ac.th/jspui/handle/123456789/14380 https://www.scopus.com/inward/record.uri?eid=2-s2.0-84857059728&doi=10.1007%2fs00436-011-2532-z&partnerID=40&md5=221f7a69f0ec7c272a5ce7d65ed12488 |
| ISSN: | 9320113 |
| Appears in Collections: | Scopus 1983-2021 |
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