pubmed-article:3435476 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:3435476 | lifeskim:mentions | umls-concept:C0003483 | lld:lifeskim |
pubmed-article:3435476 | lifeskim:mentions | umls-concept:C0009968 | lld:lifeskim |
pubmed-article:3435476 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
pubmed-article:3435476 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:3435476 | lifeskim:mentions | umls-concept:C1515655 | lld:lifeskim |
pubmed-article:3435476 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:3435476 | pubmed:dateCreated | 1988-3-15 | lld:pubmed |
pubmed-article:3435476 | pubmed:abstractText | Cu2Zn2-superoxide dismutase (CuZn-SOD) was purified from chicken liver. The liver enzyme had a subunit Mr of 16900 and contained equimolar amounts of copper and zinc [0.26% (w/w) for each]. Aortic CuZn-SOD had the same Mr as estimated by gel filtration and cross-reacted with antibodies to the liver enzyme. Both enzymes were inhibited by 1.0 mM-NaCN. Within 24-72 h after hatching, total SOD activity in aorta rose 3-fold over the day-1 level and stayed elevated for 10 days. With low dietary copper, the total SOD activity rose as before, but then decayed progressively to non-detectable levels in 10 days. Both the cyanide-sensitive (CuZn-SOD) and insensitive (mangano-SOD) activities fell, but not at the same rate. When the 10-day-old deficient chicks were injected with 0.5 mumol of CuSO4 intraperitoneally, SOD activity in aorta was restored to control levels in about 8 h. Despite non-measurable SOD activity in aorta, extracts from the 15-day-old-deficient-chick tissue contained as much, or slightly more, immunoreactive CuZn-SOD protein as age-matched control tissue. The data show clearly that dietary copper regulates SOD activity in the aortas of young developing animals. They further suggest that a copper deficiency suppresses CuZn-SOD activity without inhibiting synthesis or accumulation of the CuZn protein in this tissue. | lld:pubmed |
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pubmed-article:3435476 | pubmed:language | eng | lld:pubmed |
pubmed-article:3435476 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3435476 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:3435476 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:3435476 | pubmed:month | Dec | lld:pubmed |
pubmed-article:3435476 | pubmed:issn | 0264-6021 | lld:pubmed |
pubmed-article:3435476 | pubmed:author | pubmed-author:HarrisE DED | lld:pubmed |
pubmed-article:3435476 | pubmed:author | pubmed-author:DameronC TCT | lld:pubmed |
pubmed-article:3435476 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:3435476 | pubmed:day | 15 | lld:pubmed |
pubmed-article:3435476 | pubmed:volume | 248 | lld:pubmed |
pubmed-article:3435476 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:3435476 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:3435476 | pubmed:pagination | 663-8 | lld:pubmed |
pubmed-article:3435476 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:3435476 | pubmed:year | 1987 | lld:pubmed |
pubmed-article:3435476 | pubmed:articleTitle | Regulation of aortic CuZn-superoxide dismutase with copper. Effects in vivo. | lld:pubmed |
pubmed-article:3435476 | pubmed:affiliation | Department of Biochemistry and Biophysics, Texas A & M University, College Station 77843-2128. | lld:pubmed |
pubmed-article:3435476 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:3435476 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:3435476 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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