Linked Life Data

6513990

Source:http://linkedlifedata.com/resource/pubmed/id/6513990

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1985-2-11
pubmed:abstractText
An NADH-cytochrome c reductase (complex I-III) was isolated from Ascaris suum muscle mitochondria. The enzyme preparation catalyzed the reduction of 1.68 mumol cytochrome c min-1 mg-1 protein at 25 degrees C with NADH but not with NADPH, and retained its sensitivity to rotenone, piericidin A and 2-heptyl-4-hydroxyquinoline-N-oxide as with the submitochondrial particles. The isolated complex I-III, essentially free of succinate-cytochrome c reductase and cytochrome c oxidase, consisted of fourteen polypeptides with apparent molecular weights ranging from 76 000 to 12 000. The complex I-III contained three cytochromes, b-559.5, b-563 and c1-550.5 and Pigment-558 at concentrations of 1.28, 0.211, 1.23 and 0.321 nmol mg-1 protein, respectively. Cytochrome b-558, a major constituent cytochrome of Ascaris mitochondria and previously suggested to participate in the fumarate reductase system, was not fractionated in the complex I-III. Localization of the cytochromes in Ascaris electron transfer complexes is discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0166-6851
pubmed:author
pubmed:issnType
Print
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
121-34
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Electron transfer complexes of Ascaris suum muscle mitochondria: I. Characterization of NADH-cytochrome c reductase (complex I-III), with special reference to cytochrome localization.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't