Linked Life Data

2736251

Source:http://linkedlifedata.com/resource/pubmed/id/2736251

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1989-8-3
pubmed:abstractText
Electron-transfer flavoprotein was purified to apparent homogeneity from mitochondria of the parasitic nematode, Ascaris suum. The native molecular weight of the enzyme was 70,000, as estimated by gel filtration, and it migrated as two bands with apparent subunit molecular weights of 37,000 and 31,500 during sodium dodecylsulfate polyacrylamide gel electrophoresis. The enzyme exhibited an absorption coefficient for the bound FAD of 13.5 mM-1.cm-1 at 436 nm and a protein/flavin (270 nm/436 nm) ratio of 5.6. While the ascarid enzyme is similar to its mammalian counterpart, physiologically it functions in the reverse direction, shuttling reducing power from the electron-transport chain to a soluble 2-methyl branched-chain enoyl CoA reductase. Indeed, when A. suum submitochondrial particles were incubated with NADH, 2-methylcrotonyl-CoA and purified A. suum 2-methyl branched-chain enoyl-CoA reductase, 2-methylbutyryl-CoA formation was proportional to the amount of electron-transfer flavoprotein added.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
975
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
127-31
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Electron-transfer flavoprotein from anaerobic Ascaris suum mitochondria and its role in NADH-dependent 2-methyl branched-chain enoyl-CoA reduction.
pubmed:affiliation
Department of Biology, University of Toledo, OH 43606.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.