Linked Life Data

3997810

Source:http://linkedlifedata.com/resource/pubmed/id/3997810

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1985-6-27
pubmed:abstractText
A protein has been purified from rat liver cytosol which promoted GSH-responsive iodothyronine 5'-deiodinase activities in rat kidney microsomes. The factor behaved as a basic protein with an Mr of 11,000. It was active as a GSH-disulfide transhydrogenase with beta-hydroxyethyl disulfide as an acceptor and was also active in stimulating calf thymus ribonucleotide reductase with one-third the potency of native calf thymus glutaredoxin. Another basic protein, which degraded iodothyronines oxidatively, was also identified in the cytosolic preparations; this co-purified with soluble protein factor in the earlier purification stages and was partially separated from this factor by CM-cellulose chromatography. The glutaredoxin-like protein present in rat liver and kidney cytosol could provide a physiologic regulatory mechanism for GSH-dependent 5'-monodeiodination of iodothyronines.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
260
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6012-9
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Purification and characterization of a cytosolic protein enhancing GSH-dependent microsomal iodothyronine 5'-monodeiodination.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.