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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
2006-2-14
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pubmed:abstractText |
Human extracellular superoxide dismutase (EC-SOD) is involved in the defence against oxidative stress induced by the superoxide radical. The protein is a homotetramer stabilised by hydrophobic interactions within the N-terminal region. During the purification of EC-SOD from human aorta, we noticed that material with high affinity for heparin-Sepharose formed not only a tetramer but also an octamer. Analysis of the thermodynamic stability of the octamer suggested that the C-terminal region is involved in formation of the quaternary structure. In addition, we show that the octamer is composed of both aEC-SOD and iEC-SOD folding variants. The presence of the EC-SOD octamer with high affinity may represent a way to influence the local concentration of EC-SOD to protect tissues specifically sensitive to oxidative damage.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16469315-10329680,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16469315-10964700,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16469315-11705698,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16469315-11861638,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16469315-12147226,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16469315-12225954,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16469315-12885586,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16469315-14615576,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16469315-14736885,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16469315-15044467,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16469315-1517248,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16469315-15298984,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16469315-15518578,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16469315-225498,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16469315-3223905,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16469315-3593249,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16469315-362127,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16469315-7574505,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16469315-8227019,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16469315-8375691,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16469315-8394057,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16469315-8547348,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16469315-8643556,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16469315-8694786,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16469315-9143334,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16469315-9385637
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
580
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1485-9
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
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pubmed:year |
2006
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pubmed:articleTitle |
Extracellular superoxide dismutase exists as an octamer.
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pubmed:affiliation |
Center for Insoluble Protein Structures (inSPIN), Department of Molecular Biology, University of Aarhus, Gustav Wieds Vej 10C, DK-8000 Aarhus C, Denmark.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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