Linked Life Data

12755695

Source:http://linkedlifedata.com/resource/pubmed/id/12755695

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2003-5-20
pubmed:abstractText
As a first step toward developing a zebrafish model for investigating the role of sulfation in counteracting environmental estrogenic chemicals, we have embarked on the identification and characterization of cytosolic sulfotransferases (STs) in zebrafish. By searching the zebrafish expressed sequence tag database, we have identified two cDNA clones encoding putative cytosolic STs. These two zebrafish ST cDNAs were isolated and subjected to nucleotide sequencing. Sequence data revealed that the two zebrafish STs are highly homologous, being approximately 82% identical in their amino acid sequences. Both of them display approximately 50% amino acid sequence identity to human SULT1A1, rat SULT1A1, and mouse SULT1C1 ST. These two zebrafish STs therefore appear to belong to the SULT1 cytosolic ST gene family. Recombinant zebrafish STs (designated SULT1 STs 1 and 2), expressed using the pGEX-2TK prokaryotic expression system and purified from transformed Escherichia coli cells, migrated as approximately 35 kDa proteins on SDS/PAGE. Purified zebrafish SULT1 STs 1 and 2 displayed differential sulfating activities toward a number of endogenous compounds and xenobiotics including hydroxychlorobiphenyls. Kinetic constants of the two enzymes toward two representative hydroxychlorobiphenyls, 3-chloro-4-biphenylol and 3,3',5,5'-tetrachloro-4,4'-biphenyldiol, and 3,3',5-triiodo-l-thyronine were determined. A thermostability experiment revealed the two enzymes to be relatively stable over the range 20-43 degrees C. Among 10 different divalent metal cations tested, Co2+, Zn2+, Cd2+, and Pb2+ exhibited considerable inhibitory effects, while Hg2+ and Cu2+ rendered both enzymes virtually inactive.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:volume
270
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2404-11
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed-meshheading:12755695-Amino Acid Sequence, pubmed-meshheading:12755695-Animals, pubmed-meshheading:12755695-Arylsulfotransferase, pubmed-meshheading:12755695-Biphenyl Compounds, pubmed-meshheading:12755695-Blotting, Western, pubmed-meshheading:12755695-Cations, pubmed-meshheading:12755695-Cloning, Molecular, pubmed-meshheading:12755695-Cytosol, pubmed-meshheading:12755695-DNA, Complementary, pubmed-meshheading:12755695-DNA Primers, pubmed-meshheading:12755695-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:12755695-Escherichia coli, pubmed-meshheading:12755695-Humans, pubmed-meshheading:12755695-Hydrogen-Ion Concentration, pubmed-meshheading:12755695-Kinetics, pubmed-meshheading:12755695-Molecular Sequence Data, pubmed-meshheading:12755695-Phylogeny, pubmed-meshheading:12755695-Recombinant Proteins, pubmed-meshheading:12755695-Sequence Homology, Amino Acid, pubmed-meshheading:12755695-Sulfotransferases, pubmed-meshheading:12755695-Temperature, pubmed-meshheading:12755695-Zebrafish
pubmed:year
2003
pubmed:articleTitle
Sulfation of hydroxychlorobiphenyls. Molecular cloning, expression, and functional characterization of zebrafish SULT1 sulfotransferases.
pubmed:affiliation
Biomedical Research Center, The University of Texas Health Center, Tyler, Texas 75708, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't