title: Isolation and characterization of a novel microsomal membrane-bound phenol sulfotransferase from bovine liver.
abstract: A novel phenol sulfotransferase (PST) was detected in bovine liver microsomal membrane fraction. The enzyme was found to be capable of catalyzing the sulfation of simple phenolic compounds, with 3'-phosphoadenosine-5'-phosphosulfate as the sulfate donor. Detergent extracted PST showed a pH optimum of 5.7 and, among the simple phenols tested, the PST exhibited highest activity toward alpha-naphthol. No activities were detected when tyrosine and its derivatives were used as substrates. Both 2,6-dichloro-4-nitrophenol and chlorpromazine were capable of inhibiting the activity of the PST toward p-nitrophenol with inhibition Coefficient50 values of 100 nM and 4 mM, respectively.
authors.affiliation: Department of Biological Resource Sciences, Miyazaki University, Japan.
authors.forename: P H
authors.initials: PH
authors.lastname: Fernando
authors.forename: Y
authors.initials: Y
authors.lastname: Sakakibara
authors.forename: S
authors.initials: S
authors.lastname: Nakatsu
authors.forename: M
authors.initials: M
authors.lastname: Suiko
authors.forename: J R
authors.initials: JR
authors.lastname: Han
authors.forename: M C
authors.initials: MC
authors.lastname: Liu
mesh_terms: D000818:Animals; D015239:Arylsulfotransferase / Q000302:isolation & purification*; D002417:Cattle; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007425:Intracellular Membranes / Q000201:enzymology; D008565:Membrane Proteins / Q000302:isolation & purification*; D008862:Microsomes, Liver / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D008565:Membrane Proteins; D015239:Arylsulfotransferase