Molecular Characterization of a Human Aryl Sulfotransferase cDNA

Zhu X.Y., Veronese M.E., Sansom L.N. and Mcmanus M.E. (1993) Molecular Characterization of a Human Aryl Sulfotransferase cDNA. Biochemical and Biophysical Research Communications, 192 2: 671-676. doi:10.1006/bbrc.1993.1467

Author Zhu X.Y.
Veronese M.E.
Sansom L.N.
Mcmanus M.E.
Title Molecular Characterization of a Human Aryl Sulfotransferase cDNA
Journal name Biochemical and Biophysical Research Communications   Check publisher's open access policy
ISSN 0006-291X
Publication date 1993-04-30
Sub-type Article (original research)
DOI 10.1006/bbrc.1993.1467
Open Access Status Not yet assessed
Volume 192
Issue 2
Start page 671
End page 676
Total pages 6
Language eng
Subject 1312 Molecular Biology
1304 Biophysics
1303 Specialist Studies in Education
Abstract A full-length aryl sulfotransferase cDNA was isolated from a human liver cDNA library. It was 1155 bp long containing a coding region of 885 basepairs encoding a cytosolic protein (Mr 34178 Da) of 295 amino acids. This human cDNA shared 80% homology to the rat aryl sulfotransferase cDNA, 58% to the bovine and rat oestrogen sulfotransferase cDNAs, 53% to the rat hydroxysteroid sulfotransferase cDNA and 51% to the human liver dehydroepiandrosterone sulfotransferase cDNA over its whole 885 bp coding region. The deduced amino acid sequence of this human cDNA was 79% homologous to that of the rat aryl sulfotransferase cDNA and the putative common-substrate binding site motif GXXGXXK of the sulfotransferases has been conserved in this human amino acid sequence. At least two sizes of this human aryl sulfotransferase mRNA were detected in the human liver and lung.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Scopus Import - Archived
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Citation counts: TR Web of Science Citation Count  Cited 76 times in Thomson Reuters Web of Science Article | Citations
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