Linked Life Data

10375162

Source:http://linkedlifedata.com/resource/pubmed/id/10375162

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1999-8-9
pubmed:abstractText
Sulfotransferases (ST) are contained as multiple forms in human tissues with overlapping substrate specificities. To identify a form which contributes to the metabolism of 3, 3',5-triiodothyronine (T3), the functional properties of human STs were compared using recombinant STs, ST1A3, ST1A5, ST1B2, ST1E4 and ST2A3. ST1B2 showed a high affinity (Km 46.2 microM) for T3 sulfation, whereas ST1A3, ST1A5, ST1E4 and ST2A3 showed high affinities to p-nitrophenol (Km 0.4 microM), dopamine (Km 7.1 microM), beta-estradiol (Km 0.3 microM) and dehydroepiandrosterone (Km 3.3 microM), respectively. In Western blotting using antibodies raised against an individual ST, hepatic absolute amounts of these STs were determined. The content of ST1B2 in human liver correlated well with T3 sulfation activities in human liver (r=0.96). These results indicate that ST1B2 is biochemically distinct from other forms of ST, and is involved in the metabolism of T3 in human. In addition, studies of thermal stability and 2,6-dichloro-4-nitrophenol (DCNP) inhibition showed that ST1B2 was thermostable and more DCNP resistant than other forms of ST. Affinities for a co-factor, phosphoadenosine 5'-phosphosulfate, also differed 9-fold among 5 different forms of ST.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0918-6158
pubmed:author
pubmed:issnType
Print
pubmed:volume
22
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
446-52
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Enzymatic characterization of human cytosolic sulfotransferases; identification of ST1B2 as a thyroid hormone sulfotransferase.
pubmed:affiliation
Division of Drug Metabolism and Molecular Toxicology, Faculty of Pharmaceutical Sciences, Tohoku University, Sendai, Japan.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't