Linked Life Data

2372296

Source:http://linkedlifedata.com/resource/pubmed/id/2372296

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1990-8-21
pubmed:abstractText
In order to resolve questions concerning the in situ structure of the thyrotropin (TSH) receptor, [35S]methionine-labeled thyroid cell preparations were detergent solubilized and proteins exhibiting TSH-dependent binding to TSH-Sepharose were identified. Two such proteins, 43 and 70 kd, are identified in this report as gamma-actin and a member of the heat shock 70 protein family, respectively, based on the microsequence of two peptides from each. Identification of the former was confirmed by Western blotting and immunostaining using anti-actin, the latter by its ability to bind [32P]ATP, a characteristic feature of this family of proteins. The results suggest that TSH-cross linking reports defining TSH receptor subunits should be viewed with caution in the absence of comparative sequence data; consideration must, however, be given to the existence of receptor associated proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
170
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
351-8
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
A microsequencing approach to identify proteins which appear to interact with thyrotropin in rat FRTL-5 thyroid cells.
pubmed:affiliation
Section on Cell Regulation, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.
pubmed:publicationType
Journal Article