pubmed-article:11926067 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:11926067 | lifeskim:mentions | umls-concept:C0036025 | lld:lifeskim |
pubmed-article:11926067 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
pubmed-article:11926067 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
pubmed-article:11926067 | lifeskim:mentions | umls-concept:C0205474 | lld:lifeskim |
pubmed-article:11926067 | lifeskim:mentions | umls-concept:C1325651 | lld:lifeskim |
pubmed-article:11926067 | lifeskim:mentions | umls-concept:C0003320 | lld:lifeskim |
pubmed-article:11926067 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:11926067 | lifeskim:mentions | umls-concept:C1179435 | lld:lifeskim |
pubmed-article:11926067 | lifeskim:mentions | umls-concept:C1264633 | lld:lifeskim |
pubmed-article:11926067 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
pubmed-article:11926067 | pubmed:issue | 1-2 | lld:pubmed |
pubmed-article:11926067 | pubmed:dateCreated | 2002-4-2 | lld:pubmed |
pubmed-article:11926067 | pubmed:abstractText | We analyzed the protein components contained in the mitochondrial nucleoid (mt-nucleoid) fraction of the yeast Saccharomyces cerevisiae. Immunoblotting with anti-Abf2p antibody demonstrated the association of Abf2p, a major mitochondrial DNA-binding protein, with the mt-nucleoids. In contrast, porin and cytochrome c oxidase subunit III (CoxIIIp) were not detected by immunoblotting in the mt-nucleoid fraction. The YMN-1 monoclonal antibody recognized a 48 kDa protein of the mt-nucleoid fraction. The N-terminal amino acid sequence of the protein and immunological evidence showed that the YMN-1 monoclonal antibody recognizes dihydrolipoyl transsuccinylase (KE2), which is one of the constituents of the alpha-ketoglutarate dehydrogenase complex (KGDC). alpha-Ketoglutarate dehydrogenase (KE1) and dihydrolipoyl dehydrogenase (E3), which are other subunits of KGDC, were also detected in the mt-nucleoid fraction. An enzyme assay of the mt-nucleoid fraction showed that cytochrome c oxidase and fumarase activity were barely detected in the fraction, but the specific activity of KGDC in the mt-nucleoid fraction was relatively high and was approximately 60% of the specific activity in the mitochondrial fraction. Three components of KGDC were detected in the DNA-binding protein fractions after DNA-cellulose column chromatography of mt-nucleoid proteins. These results suggested that a part of KGDC in the mitochondrial matrix is associated with mt-nucleoids in vivo. | lld:pubmed |
pubmed-article:11926067 | pubmed:language | eng | lld:pubmed |
pubmed-article:11926067 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11926067 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:11926067 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11926067 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11926067 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11926067 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11926067 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11926067 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11926067 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11926067 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11926067 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11926067 | pubmed:month | Feb | lld:pubmed |
pubmed-article:11926067 | pubmed:issn | 0033-183X | lld:pubmed |
pubmed-article:11926067 | pubmed:author | pubmed-author:SatoHH | lld:pubmed |
pubmed-article:11926067 | pubmed:author | pubmed-author:TamuraMM | lld:pubmed |
pubmed-article:11926067 | pubmed:author | pubmed-author:MiyakawaII | lld:pubmed |
pubmed-article:11926067 | pubmed:author | pubmed-author:TachifujiAA | lld:pubmed |
pubmed-article:11926067 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:11926067 | pubmed:volume | 219 | lld:pubmed |
pubmed-article:11926067 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11926067 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11926067 | pubmed:pagination | 51-8 | lld:pubmed |
pubmed-article:11926067 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:11926067 | pubmed:meshHeading | pubmed-meshheading:11926067... | lld:pubmed |
pubmed-article:11926067 | pubmed:year | 2002 | lld:pubmed |
pubmed-article:11926067 | pubmed:articleTitle | Identification of the YMN-1 antigen protein and biochemical analyses of protein components in the mitochondrial nucleoid fraction of the yeast Saccharomyces cerevisiae. | lld:pubmed |
pubmed-article:11926067 | pubmed:affiliation | Department of Physics, Biology and Informatics, Faculty of Science, Yamaguchi University, Yamaguchi, 753-8512, Japan. | lld:pubmed |
pubmed-article:11926067 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:11926067 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:854681 | entrezgene:pubmed | pubmed-article:11926067 | lld:entrezgene |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11926067 | lld:pubmed |