Source:http://linkedlifedata.com/resource/pubmed/id/12876653
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2003-7-23
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pubmed:abstractText |
Copper/zinc superoxide dismutase was cloned from the zebrafish ( Danio rerio). The full coding region of the zebrafish superoxide dismutase (ZSOD) complementary DNA was ligated with pET-20b(+) and successfully expressed in Escherichia coli strain AD494(DE3)pLysS. The active enzyme was purified by His tagging. The ZSOD yield was 6 mg from 0.2 L of E. coli culture, and the specific activity was 2000 U/mg as assayed using a RANSOD kit. The enzyme stability was characterized by reaction to temperature, pH, and detergent treatment. The results showed enzyme activity was still active after heat treatment at 70 degrees C for 10 minutes, resistant to pH treatment from 2.3 to 12, and resistant to treatment with sodium dodecyl sulfate (SDS) under 4%. In addition, the recombinant ZSOD was used to protect fish from 100 ppm of paraquat-induced oxidative injury by soaking fish larva in 55 micro g/ml SOD enzyme. The results were significant.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Herbicides,
http://linkedlifedata.com/resource/pubmed/chemical/Paraquat,
http://linkedlifedata.com/resource/pubmed/chemical/Superoxide Dismutase,
http://linkedlifedata.com/resource/pubmed/chemical/Zebrafish Proteins
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pubmed:status |
MEDLINE
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pubmed:issn |
1436-2228
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
167-73
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12876653-Animals,
pubmed-meshheading:12876653-Cloning, Molecular,
pubmed-meshheading:12876653-DNA, Complementary,
pubmed-meshheading:12876653-Escherichia coli,
pubmed-meshheading:12876653-Herbicides,
pubmed-meshheading:12876653-Larva,
pubmed-meshheading:12876653-Oxidative Stress,
pubmed-meshheading:12876653-Paraquat,
pubmed-meshheading:12876653-Superoxide Dismutase,
pubmed-meshheading:12876653-Zebrafish,
pubmed-meshheading:12876653-Zebrafish Proteins
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pubmed:articleTitle |
Characterization of fish Cu/Zn-superoxide dismutase and its protection from oxidative stress.
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pubmed:affiliation |
Graduate Institute of Life Sciences, National Defense Medical Center, Taiwan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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