Isolation and characterization of a novel microsomal membrane-bound phenol sulfotransferase from bovine liver.
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.
Fernando
P H
PH
Department of Biological Resource Sciences, Miyazaki University, Japan.
Sakakibara
Y
Y
Nakatsu
S
S
Suiko
M
M
Han
J R
JR
Liu
M C
MC
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
D008565:Membrane Proteins; D015239:Arylsulfotransferase