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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
20
|
pubmed:dateCreated |
1981-1-26
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pubmed:abstractText |
One to two molecules of tightly bound cardiolipin are associated with resolved fractions of cytochrome oxidase containing subunits I to III or I to IV. Large scale isolation of subunits I to IV indicates the presence of approximately 0.5 molecule of cardiolipin per molecule of subunit I. Lipoprotein staining of sodium dodecyl sulfate/urea/acrylamide gels of cytochrome oxidase support the findings that subunit I is a lipoprotein. The resistance of this tightly bound cardiolipin to organic solvent extraction suggests a specific association of some tenacity with the protein.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Oct
|
pubmed:issn |
0021-9258
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
25
|
pubmed:volume |
255
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
9967-70
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading | |
pubmed:year |
1980
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pubmed:articleTitle |
The localization of tightly bound cardiolipin in cytochrome oxidase.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|