Correlation of phenol sulphotransferase activities in the liver and platelets of rat

Abstract

Phenol sulphotransferase (PST) activity in rat platelet cytosol for p-nitrophenol (PNP) sulphation was found to have a similar dependence on PNP concentration and thermostability to that in rat liver cytosol. The activities of PST isoenzyme for the sulphation in the microM range of PNP in rat platelets and rat liver were significantly correlated. Thus, measurement of PST activity in platelets could be a useful and practical method for predicting this activity in liver.

Interaction of the Brain-Selective Sulfotransferase SULT4A1 with Other Cytosolic Sulfotransferases: Effects on Protein Expression and Function

“…The SULT1A family consists of 1A1, 1A2, 1A3 and 1A4 where the 1A3 and 1A4 genes appear to have arisen from a segmental duplication that encode the same protein (Hildebrandt et al, 2004). The SULT1A sulfotransferases are expressed widely with high abundance in the liver, lung, brain, skin, platelets, gastrointestinal tissues and kidney (Maus et al, 1982;Campbell et al, 1987;Heroux et al, 1989;Cappiello et al, 1990;Falany et al, 1990;Nakamura et al, 1990;Hume and Coughtrie, 1994;Kudlacek et al, 1995). In humans, the SULT1A subfamily members SULT1A1 and SULT1A2 primarily conjugate xenobiotics and have a role in the activation of carcinogens (Glatt, 2000), although they also sulfonated endogenous substrates (Falany, 1997;Strott, 2002).…”