Multiple forms of phenolsulphotransferase in human tissues: selective inhibition by dichloronitrophenol.

Evidence is presented for two functional forms of phenolsulphotransferase in human tissues: (1) activity ratios, using dopamine and phenol as substrates, varied 30-fold between different tissues, whereas the dopamine to tyramine activity ratio was relatively constant; (2) incubation at 37 degrees caused a selective decrease in activity towards dopamine compared with phenol; and (3) phenol sulphoconjugation was selectively inhibited by dichloronitrophenol and pentachlorophenol compared with that of dopamine and tyramine. The two forms, which have been designated M (monoamines) and P (phenol), were both present in platelets, jejunum, adrenal and brain.