Linked Life Data

8408083

Source:http://linkedlifedata.com/resource/pubmed/id/8408083

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
29
pubmed:dateCreated
1993-11-18
pubmed:abstractText
The magnesium ion in bovine heart cytochrome c oxidase can be depleted up to 75% by heat treatment of the enzyme at 43 degrees C followed by dialysis against EDTA buffer solution. The magnesium-depleted enzyme so obtained retains 40% of the activity of the native enzyme. This is the first attempt to deplete magnesium ion from bovine heart cytochrome c oxidase without denaturation of the protein. Magnesium depletion exposes at least one carboxyl group on subunit IV for labeling by N-cyclohexyl-N'-(4-dimethylaminonaphthyl)carbodiimide (NCD-4). The NCD-4 labeling of subunit IV of the magnesium-depleted enzyme is significantly enhanced relative to what is observed for the native and heat-treated oxidase, suggesting that the magnesium ion is located in subunit IV with at least one carboxyl ligand. By comparing the activity of the magnesium-depleted enzyme with that of a control sample of heat-treated oxidase, the influence of divalent magnesium on the activity of the enzyme is assessed.
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
15
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
22210-4
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
The subunit location of magnesium in cytochrome c oxidase.
pubmed:affiliation
Arthur Amos Noyes Laboratory of Chemical Physics, California Institute of Technology, Pasadena 91125.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.