Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6
|
| pubmed:dateCreated |
1995-7-17
|
| pubmed:databankReference | |
| pubmed:abstractText |
A distinct human estrogen sulfotransferase (hEST-1) cDNA has been isolated from a human liver lambda Zap cDNA library using a PCR procedure. The enzymatically active protein has been expressed in two bacterial expression systems and the kinetic and immunologic properties of the enzyme have been characterized. The full-length cDNA for hEST-1 is 994 base pairs in length and encodes a 294 amino acid protein with a calculated molecular mass of 35,123 Da. Purified hEST-1 migrated with an apparent molecular mass of 35,000 Da during SDS-polyacrylamide gel electrophoresis. Immunoblot analysis of hEST-1 expressed in E. coli with a rabbit anti-hEST-1 antibody yields a band of approximately 35,000 Da. The anti-hEST-1 antibody also detects a single band in human liver and jejunum cytosol which migrates with the same molecular mass as expressed hEST-1. There was also no cross-reactivity of hEST-1 with rabbit anti-hP-PST or rabbit anti-hDHEA-ST antibodies upon immunoblot analysis. hEST-1 was expressed in bacteria and purified to homogeneity. Expressed hEST-1 activity has a significantly greater affinity for estrogen sulfation than that found for the other human STs which conjugate estrogens. hEST-1 maximally sulfates beta-estradiol and estrone at concentrations of 20 nM. hEST-1 also sulfates dehydroepiandrosterone, pregnenolone, ethinylestradiol, and 1-naphthol, at significantly higher concentrations; however, cortisol, testosterone and dopamine are not sulfated. The results presented in this paper describe the expression and characterization of a human EST distinct from other human STs which sulfate estrogens. The high affinity of hEST-1 for estrogens indicates that this ST may be important in both the metabolism of estrogens and in the regulation of their activities.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jun
|
| pubmed:issn |
0960-0760
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
52
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
529-39
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:7779757-Amino Acid Sequence,
pubmed-meshheading:7779757-Animals,
pubmed-meshheading:7779757-Base Sequence,
pubmed-meshheading:7779757-DNA, Complementary,
pubmed-meshheading:7779757-Escherichia coli,
pubmed-meshheading:7779757-Estrogens,
pubmed-meshheading:7779757-Gene Expression,
pubmed-meshheading:7779757-Humans,
pubmed-meshheading:7779757-Kinetics,
pubmed-meshheading:7779757-Liver,
pubmed-meshheading:7779757-Molecular Sequence Data,
pubmed-meshheading:7779757-Molecular Weight,
pubmed-meshheading:7779757-Polymerase Chain Reaction,
pubmed-meshheading:7779757-Rabbits,
pubmed-meshheading:7779757-Sequence Homology, Amino Acid,
pubmed-meshheading:7779757-Species Specificity,
pubmed-meshheading:7779757-Substrate Specificity,
pubmed-meshheading:7779757-Sulfotransferases
|
| pubmed:year |
1995
|
| pubmed:articleTitle |
Bacterial expression and characterization of a cDNA for human liver estrogen sulfotransferase.
|
| pubmed:affiliation |
Department of Pharmacology and Toxicology, University of Alabama at Birmingham 35294, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|