Linked Life Data

7911463

Source:http://linkedlifedata.com/resource/pubmed/id/7911463

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-7-12
pubmed:abstractText
An extramitochondrial acetyl-CoA hydrolase [EC 3.1.2.1] in the rat liver, which is stimulated by ATP and inhibited by ADP, is known to be extremely cold-labile. During subcellular fractionations at low temperatures (2-4 degrees C), most of the enzyme activity was lost; however, most could be recovered by rewarming at 37 degrees C in the presence of a high concentration of potassium phosphate. This enabled us to measure the activities of cold-treated samples. The majority of the ATP-stimulated and ADP-inhibited acetyl-CoA hydrolase activity in rat livers was detected in the cytosolic fraction and small amounts were detected in the peroxisomal fraction. The activity of peroxisomal ATP-stimulated acetyl-CoA hydrolase was not noticeably increased after clofibrate-treatment. However, the cytosolic activity greatly increased after clofibrate treatment. The activity in the isolated peroxisomal fraction per g of liver was about 5% of that in the cytosolic fraction of liver from the control and about 2% in that from clofibrate-treated rats. Besides having similar nucleotide (ATP and ADP) sensitivity and cold lability, the enzyme protein in the peroxisomal fraction migrated to the same position as the cytosolic acetyl-CoA hydrolase based on Western blot analysis with antibody against purified acetyl-CoA hydrolase from rat liver cytosol. These results suggest that the peroxisomal enzyme and cytosolic enzyme may be the same entity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
115
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
328-32
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Subcellular distribution of ATP-stimulated and ADP-inhibited acetyl-CoA hydrolase in livers from control and clofibrate-treated rats: comparison of the cytosolic and peroxisomal enzyme.
pubmed:affiliation
Department of Oncology, Osaka University Medical School.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't