| pubmed-article:15882838 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15882838 | lifeskim:mentions | umls-concept:C0699040 | lld:lifeskim |
| pubmed-article:15882838 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:15882838 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:15882838 | lifeskim:mentions | umls-concept:C0439064 | lld:lifeskim |
| pubmed-article:15882838 | lifeskim:mentions | umls-concept:C0205171 | lld:lifeskim |
| pubmed-article:15882838 | lifeskim:mentions | umls-concept:C0682753 | lld:lifeskim |
| pubmed-article:15882838 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:15882838 | pubmed:dateCreated | 2005-6-13 | lld:pubmed |
| pubmed-article:15882838 | pubmed:abstractText | Reduction of the cell-impermeable tetrazolium salt WST-1 has been used to characterise two plasma membrane NADH oxidoreductase activities in human cells. The trans activity, measured with WST-1 and the intermediate electron acceptor mPMS, utilises reducing equivalents from intracellular sources, while the surface activity, measured with WST-1 and extracellular NADH, is independent of intracellular metabolism. Whether these two activities involve distinct proteins or are inherent to a single protein is unclear. In this work, we have attempted to address this question by examining the relationship between the trans and surface WST-1-reducing activities and a third well-characterised family of cell surface oxidases, the ECTO-NOX proteins. Using blue native-polyacrylamide gel electrophoresis, we have identified a complex in the plasma membranes of human 143B osteosarcoma cells responsible for the NADH-dependent reduction of WST-1. The dye-reducing activity of the 300 kDa complex was attributed to a 70 kDa NADH oxidoreductase activity that cross-reacted with antisera against the ECTO-NOX protein CNOX. Differences in enzyme activities and inhibitor profiles between the WST-1-reducing NADH oxidoreductase enzyme in the presence of NADH or mPMS and the ECTO-NOX family are reconciled in terms of the different purification methods and assay systems used to study these proteins. | lld:pubmed |
| pubmed-article:15882838 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15882838 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15882838 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15882838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15882838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15882838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15882838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15882838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15882838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15882838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15882838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15882838 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15882838 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:15882838 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:15882838 | pubmed:author | pubmed-author:BerridgeMicha... | lld:pubmed |
| pubmed-article:15882838 | pubmed:author | pubmed-author:ScarlettDebbi... | lld:pubmed |
| pubmed-article:15882838 | pubmed:author | pubmed-author:HerstPatries... | lld:pubmed |
| pubmed-article:15882838 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15882838 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:15882838 | pubmed:volume | 1708 | lld:pubmed |
| pubmed-article:15882838 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15882838 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15882838 | pubmed:pagination | 108-19 | lld:pubmed |
| pubmed-article:15882838 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:15882838 | pubmed:meshHeading | pubmed-meshheading:15882838... | lld:pubmed |
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| pubmed-article:15882838 | pubmed:meshHeading | pubmed-meshheading:15882838... | lld:pubmed |
| pubmed-article:15882838 | pubmed:meshHeading | pubmed-meshheading:15882838... | lld:pubmed |
| pubmed-article:15882838 | pubmed:meshHeading | pubmed-meshheading:15882838... | lld:pubmed |
| pubmed-article:15882838 | pubmed:meshHeading | pubmed-meshheading:15882838... | lld:pubmed |
| pubmed-article:15882838 | pubmed:meshHeading | pubmed-meshheading:15882838... | lld:pubmed |
| pubmed-article:15882838 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15882838 | pubmed:articleTitle | Multiple proteins with single activities or a single protein with multiple activities: the conundrum of cell surface NADH oxidoreductases. | lld:pubmed |
| pubmed-article:15882838 | pubmed:affiliation | Malaghan Institute of Medical Research, PO Box 7060, Wellington, New Zealand. | lld:pubmed |
| pubmed-article:15882838 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15882838 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:55068 | entrezgene:pubmed | pubmed-article:15882838 | lld:entrezgene |
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