Linked Life Data

3051830

Source:http://linkedlifedata.com/resource/pubmed/id/3051830

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1988-11-18
pubmed:abstractText
Extrathyroidal deiodination of the thyroidal main secretory product L-T4, which may have prohormone functions, reveals hormonally active and potentially regulatory potent triiodothyronines. The regulation of these enzyme reactions is still unknown but three deiodinase isoenzymes can be classified based on their physicochemical, kinetic, pharmacological and physiological properties. The purification to homogeneity and cloning of the substrate binding 27kDa subunit of 5'-deiodinase type I is currently performed and these experiments suggest a close similarity of this subunit in 5'D I and II, no evidence is found yet supporting a structural relationship to other ITH binding, transport, metabolizing or receptor proteins, in spite of a high similarity of the hormone binding sites of 5'D I and hTBPA.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0303-8173
pubmed:author
pubmed:issnType
Print
pubmed:volume
15 Suppl 1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
22-4
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Biochemistry of iodothyronine deiodination.
pubmed:affiliation
Abteilung Klinische Endokrinologie, Medizinische Hochschule Hannover, BRD.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review, Research Support, Non-U.S. Gov't