| pubmed-article:9207178 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9207178 | lifeskim:mentions | umls-concept:C0019944 | lld:lifeskim |
| pubmed-article:9207178 | lifeskim:mentions | umls-concept:C0005821 | lld:lifeskim |
| pubmed-article:9207178 | lifeskim:mentions | umls-concept:C0038563 | lld:lifeskim |
| pubmed-article:9207178 | lifeskim:mentions | umls-concept:C0171406 | lld:lifeskim |
| pubmed-article:9207178 | lifeskim:mentions | umls-concept:C0001480 | lld:lifeskim |
| pubmed-article:9207178 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:9207178 | lifeskim:mentions | umls-concept:C1948027 | lld:lifeskim |
| pubmed-article:9207178 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:9207178 | pubmed:dateCreated | 1997-7-24 | lld:pubmed |
| pubmed-article:9207178 | pubmed:abstractText | A method to prepare coupled submitochondrial particles from horse platelets is described. The method allowed us to study the protonophoric activities of both complex I and complex V following the fluorescence quenching of the monoamine 9-amino-6-chloro-2 methoxyacridine (ACMA), a probe highly sensitive to the generation of a transmembrane delta pH. We carried out a kinetic analysis of each enzyme complex studying the proton translocation and the electron transfer activities of complex I as well as the proton translocation and the ATP hydrolytic activities of complex V. A micromethod to prepare coupled submitochondrial particles from platelets might be useful to investigate cell bioenergetic damage occurring in mitochondrial diseases and ageing. | lld:pubmed |
| pubmed-article:9207178 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9207178 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9207178 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9207178 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9207178 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9207178 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9207178 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9207178 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9207178 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9207178 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:9207178 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:9207178 | pubmed:author | pubmed-author:LenazGG | lld:pubmed |
| pubmed-article:9207178 | pubmed:author | pubmed-author:GhelliAA | lld:pubmed |
| pubmed-article:9207178 | pubmed:author | pubmed-author:BaraccaAA | lld:pubmed |
| pubmed-article:9207178 | pubmed:author | pubmed-author:BucchiLL | lld:pubmed |
| pubmed-article:9207178 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9207178 | pubmed:day | 27 | lld:pubmed |
| pubmed-article:9207178 | pubmed:volume | 235 | lld:pubmed |
| pubmed-article:9207178 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9207178 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9207178 | pubmed:pagination | 469-73 | lld:pubmed |
| pubmed-article:9207178 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:9207178 | pubmed:meshHeading | pubmed-meshheading:9207178-... | lld:pubmed |
| pubmed-article:9207178 | pubmed:meshHeading | pubmed-meshheading:9207178-... | lld:pubmed |
| pubmed-article:9207178 | pubmed:meshHeading | pubmed-meshheading:9207178-... | lld:pubmed |
| pubmed-article:9207178 | pubmed:meshHeading | pubmed-meshheading:9207178-... | lld:pubmed |
| pubmed-article:9207178 | pubmed:meshHeading | pubmed-meshheading:9207178-... | lld:pubmed |
| pubmed-article:9207178 | pubmed:meshHeading | pubmed-meshheading:9207178-... | lld:pubmed |
| pubmed-article:9207178 | pubmed:meshHeading | pubmed-meshheading:9207178-... | lld:pubmed |
| pubmed-article:9207178 | pubmed:meshHeading | pubmed-meshheading:9207178-... | lld:pubmed |
| pubmed-article:9207178 | pubmed:meshHeading | pubmed-meshheading:9207178-... | lld:pubmed |
| pubmed-article:9207178 | pubmed:meshHeading | pubmed-meshheading:9207178-... | lld:pubmed |
| pubmed-article:9207178 | pubmed:meshHeading | pubmed-meshheading:9207178-... | lld:pubmed |
| pubmed-article:9207178 | pubmed:meshHeading | pubmed-meshheading:9207178-... | lld:pubmed |
| pubmed-article:9207178 | pubmed:meshHeading | pubmed-meshheading:9207178-... | lld:pubmed |
| pubmed-article:9207178 | pubmed:meshHeading | pubmed-meshheading:9207178-... | lld:pubmed |
| pubmed-article:9207178 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9207178 | pubmed:articleTitle | Protonophoric activity of NADH coenzyme Q reductase and ATP synthase in coupled submitochondrial particles from horse platelets. | lld:pubmed |
| pubmed-article:9207178 | pubmed:affiliation | Department of Biochemistry G. Moruzzi, Bologna, Italy. | lld:pubmed |
| pubmed-article:9207178 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9207178 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
