PMID: 2113604Jun 1, 1990Paper

Rat liver cytosolic hydroxysteroid sulfotransferase (sulfotransferase a) catalyzing the formation of reactive sulfate esters from carcinogenic polycyclic hydroxymethylarenes

Molecular Pharmacology
K OguraT Watabe

Abstract

Female rat liver cytosol contained at least three sulfotransferases (STs) that were separable on a DEAE-Sephadex A-50 column and transformed the carcinogen 5-hydroxymethylchrysene (5-HCR) to the potent mutagen 5-HCR sulfate. The STs also catalyzed sulfation of dehydroepiandrosterone (DHA), a typical substrate for hydroxysteroid STs. Of these three isozymes, the one (STa) with the highest 5-HCR-sulfating activity was isolated and purified (100-fold) as a homogeneous protein, in 15% yield, by successive column chromatography on agarose modified with 3'-phosphoadenosine 5'-phosphate as an affinity ligand and on Sephadex G-100. Purified STa was classified as a hydroxysteroid ST because the 5-HCR- and DHA-sulfating activities were inseparable from each other throughout the purification steps. Sulfation of 5-HCR by purified STa was competitively inhibited by DHA. STa also catalyzed sulfation of other potent carcinogens, 7-hydroxymethylbenz[a]anthracene, 7-hydroxymethyl-12-methylbenz[a]anthracene, and 7,12-dihydroxymethylbenz[a], anthrocene, to produce sulfate esters with high reactivity and mutagenicity. However, STa had no activity with 4-nitrophenol, a typical substrate for phenol STs, or with N-hydroxy-2-acetylaminofluorene. STa h...Continue Reading

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