Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1987-8-28
pubmed:abstractText
We prepared monospecific antisera in rabbits against purified rat short-, medium-, and long-chain acyl-CoA dehydrogenases, isovaleryl-CoA dehydrogenase, and ETF and tested the immunocross-reactivity to the corresponding human enzymes. Each antiserum specifically reacted with the corresponding human enzyme. When immunoprecipitates were analyzed by SDS-PAGE, the mobilities of all the human acyl-CoA dehydrogenases and ETF subunits were identical to those of the rat counterparts with a single exception. Human medium-chain acyl-CoA dehydrogenase had a mobility on SDS-PAGE slightly slower than that of rat medium-chain acyl-CoA dehydrogenase, suggesting that human medium-chain acyl-CoA dehydrogenase was 1 kDa larger than the rat counterpart. The immunocross-reactivity of the antisera, raised against the rat acyl-CoA dehydrogenases and ETF to the human counterpart, provide useful tools for the study of mutant enzymes in cells from patients with a genetic defect of acyl-CoA dehydrogenases of ETF.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0885-4505
pubmed:author
pubmed:issnType
Print
pubmed:volume
37
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
329-34
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Immunoprecipitation and electrophoretic analysis of four human acyl-CoA dehydrogenases and electron transfer flavoprotein using antibodies raised against the corresponding rat enzymes.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't