Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1981-1-26
pubmed:abstractText
The study was undertaken to examine the potential intrinsic biological activity of reverse T3 by comparing its binding to nuclear protein in vitro with that of other iodothyronines. Nuclear protein was extracted from normal pig liver using methods described for rat tissues. At 25 degrees 30% of the added 125I rT3 was specifically bound to the nuclear protein. The order of potency in displacing 125I rT3 was rT3 > 3'5'T2 > T4 > T3 > 3,3'T2 > 3,5T2. This contrasted with the order of potency in displacing 125I T3 which was T3 > T4 > 3,3'T2 > 3,5T2 > rT3 > 3'5'T2. This difference in the hierarchy of iodothyronine binding is consistent with binding of these radioligands to different components of the nuclear protein extract. These experiments demonstrate separate binding components of nuclear protein for T3 and rT3 in a thyroid hormone responsive tissue and may be relevant to the mechanism of action of thyroid hormones.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0004-945X
pubmed:author
pubmed:issnType
Print
pubmed:volume
58
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
207-12
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Binding of reverse T3 to hepatic nuclear protein.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't