Linked Life Data

204652

Source:http://linkedlifedata.com/resource/pubmed/id/204652

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1978-5-24
pubmed:abstractText
Properties of soluble high potential type iron-sulfur protein (HiPIP) from beef heart mitochondria were compared to those of aconitase from pig heart. The two proteins when purified to homogeneity by the criteria of sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis show identical light absorption characteristics. EPR signals of the HiPIP type centered at g = 2.01 when oxidized, isoelectric points at pH 8.5 to 8.6, are inseparable by SDS-polyacrylamide electrophoresis, and exhibit aconitase activity when activated by reducing agents in the presence of ferrous iron. The requirement for activation goes parallel to the intensity of the signal from the oxidized iron-sulfur cluster, i.e. the cluster is reduced in the active enzyme. We conclude that the soluble mitochondrial HiPIP is identical with aconitase. The relationships of iron to labile sulfide, molecular weight and unpaired spins in the EPR signal, and implications of our findings for the role of iron in aconitase are discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
253
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2514-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1978
pubmed:articleTitle
The soluble "high potential" type iron-sulfur protein from mitochondria is aconitase.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.