| pubmed-article:1550344 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1550344 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:1550344 | lifeskim:mentions | umls-concept:C0018787 | lld:lifeskim |
| pubmed-article:1550344 | lifeskim:mentions | umls-concept:C0026237 | lld:lifeskim |
| pubmed-article:1550344 | lifeskim:mentions | umls-concept:C1141015 | lld:lifeskim |
| pubmed-article:1550344 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:1550344 | lifeskim:mentions | umls-concept:C0205349 | lld:lifeskim |
| pubmed-article:1550344 | lifeskim:mentions | umls-concept:C1883709 | lld:lifeskim |
| pubmed-article:1550344 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:1550344 | pubmed:dateCreated | 1992-4-17 | lld:pubmed |
| pubmed-article:1550344 | pubmed:abstractText | Rat myocardial membranes exposed to free radical-generating systems exhibit both lipid peroxidation and protein alterations. The most sensitive protein, a 28-kDa polypeptide, was previously shown to increase slightly in apparent molecular weight before disappearing completely from the protein profile [N. L. Parinandi, C. W. Zwizinski, and H. H. O. Schmid (1991) Arch. Biochem. Biophys. 289, 118-123]. We now report that isolated cardiac mitochondria contain a 28-kDa protein which responds in the same manner to treatment with Cu2+/t-butylhydroperoxide. The protein exhibits several characteristic properties of the mitochondrial adenine nucleotide translocase. This assignment is supported by the finding that carboxyatractyloside, a specific inhibitor of the adenine nucleotide translocase, can prevent the oxidant-induced changes in the 28-kDa protein. Efficient purification schemes for the isolation of milligram quantities of unmodified and oxidatively altered adenine nucleotide translocase from rat heart mitochondria are described. | lld:pubmed |
| pubmed-article:1550344 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1550344 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1550344 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1550344 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1550344 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1550344 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1550344 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1550344 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1550344 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1550344 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1550344 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1550344 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1550344 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1550344 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:1550344 | pubmed:issn | 0003-9861 | lld:pubmed |
| pubmed-article:1550344 | pubmed:author | pubmed-author:SchmidH HHH | lld:pubmed |
| pubmed-article:1550344 | pubmed:author | pubmed-author:ZwizinskiC... | lld:pubmed |
| pubmed-article:1550344 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1550344 | pubmed:volume | 294 | lld:pubmed |
| pubmed-article:1550344 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1550344 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1550344 | pubmed:pagination | 178-83 | lld:pubmed |
| pubmed-article:1550344 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:1550344 | pubmed:meshHeading | pubmed-meshheading:1550344-... | lld:pubmed |
| pubmed-article:1550344 | pubmed:meshHeading | pubmed-meshheading:1550344-... | lld:pubmed |
| pubmed-article:1550344 | pubmed:meshHeading | pubmed-meshheading:1550344-... | lld:pubmed |
| pubmed-article:1550344 | pubmed:meshHeading | pubmed-meshheading:1550344-... | lld:pubmed |
| pubmed-article:1550344 | pubmed:meshHeading | pubmed-meshheading:1550344-... | lld:pubmed |
| pubmed-article:1550344 | pubmed:meshHeading | pubmed-meshheading:1550344-... | lld:pubmed |
| pubmed-article:1550344 | pubmed:meshHeading | pubmed-meshheading:1550344-... | lld:pubmed |
| pubmed-article:1550344 | pubmed:meshHeading | pubmed-meshheading:1550344-... | lld:pubmed |
| pubmed-article:1550344 | pubmed:meshHeading | pubmed-meshheading:1550344-... | lld:pubmed |
| pubmed-article:1550344 | pubmed:meshHeading | pubmed-meshheading:1550344-... | lld:pubmed |
| pubmed-article:1550344 | pubmed:meshHeading | pubmed-meshheading:1550344-... | lld:pubmed |
| pubmed-article:1550344 | pubmed:meshHeading | pubmed-meshheading:1550344-... | lld:pubmed |
| pubmed-article:1550344 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1550344 | pubmed:articleTitle | Peroxidative damage to cardiac mitochondria: identification and purification of modified adenine nucleotide translocase. | lld:pubmed |
| pubmed-article:1550344 | pubmed:affiliation | Hormel Institute, University of Minnesota, Austin 55912. | lld:pubmed |
| pubmed-article:1550344 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1550344 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1550344 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1550344 | lld:pubmed |
