Linked Life Data

3837981

Source:http://linkedlifedata.com/resource/pubmed/id/3837981

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1986-10-6
pubmed:abstractText
The properties of the thyroid hormone binding to rat heart cytosol were studied. Cytosol proteins were found to bind specifically T4 with high affinity (Ka approximately equal to 10(8)M-1) and rT3 with lower affinity (Ka approximately equal to 10(7)M-1), but they do not bind T3. The binding of both T4 and rT3 was pH dependent, however, while T4 binding had the highest values between pH 7.0 and 10, rT3 binding increased from pH 6.0 to 10.7. Divalent ions also stimulated T4 and rT3 binding. Sulfhydryl groups blocking agents such as N-ethylmaleimide (NEM) and iodoacetamide significantly decreased rT3 binding and had less profound effect on binding of T4 to cytosol proteins. The importance of free -SH groups remains unclear as dithiothreitol was found to diminish the binding of T4 and rT3.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0044-6033
pubmed:author
pubmed:issnType
Print
pubmed:volume
36
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
248-55
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
Thyroid hormone binding to the rat heart cytosol proteins.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't