PT  - JOURNAL ARTICLE
AU  - T W Wilborn
AU  - K A Comer
AU  - T P Dooley
AU  - I M Reardon
AU  - R L Heinrikson
AU  - C N Falany
TI  - Sequence analysis and expression of the cDNA for the phenol-sulfating form of human liver phenol sulfotransferase.
DP  - 1993 Jan 01
TA  - Molecular Pharmacology
PG  - 70--77
VI  - 43
IP  - 1
4099  - http://molpharm.aspetjournals.org/content/43/1/70.short
4100  - http://molpharm.aspetjournals.org/content/43/1/70.full
SO  - Mol Pharmacol1993 Jan 01; 43
AB  - A cDNA encoding the human liver phenol-sulfating form of phenol sulfotransferase (P-PST) has been isolated and characterized from a lambda Uni-Zap XR human liver cDNA library. P-PST is the major form of phenol sulfotransferase involved in drug and xenobiotic metabolism in human liver. P-PST is also responsible for the sulfation and activation of minoxidil to its therapeutically active sulfate ester. The full length cDNA, P-PST-1, is 1206 base pairs in length and encodes a 295-amino acid protein with a molecular mass of 34,097 Da. The translation sequence of P-PST-1 is 96% similar to the amino acid sequences of five peptides derived from the purified protein. In vitro transcription and translation of P-PST-1 generated a protein that comigrates with immunoreactive P-PST from human liver. Significant increases in sulfotransferase activity toward two P-PST-specific substrates, minoxidil and 4-nitrophenol, were detected in cytosol prepared from COS-7 cells transfected with P-PST-1 in the expression vector p-SV-SPORT-1. Northern blot analysis of human liver RNA detected a transcript of approximately 1300 nucleotides in length. Characterization of P-PST at the molecular level provides insight into the structure and heterogeneity of this major class of drug-metabolizing enzymes.