Enzymatic sulfation of Triton X-100

Triton X-100 increased incorporation of [35S]sulfate into lipid-soluble substances when it was incubated with the high-speed supernatant enzymes of bovine or sheep adrenal cortex or rat liver, kidney or brain. Thin-layer chromatographic comparison of these compounds with chemically synthesized standards indicated that sulfate derivatives of Triton X-100 oligomers were formed in the liver and adrenal supernatant enzyme preparations. Further evidence for Triton X-100 sulfation by these enzymes was obtained by the use of [3H]Triton X-100 and purified Triton X-100 oligomers. No discernible sulfation of Triton X-100 occurred in kidney or brain high-speed supernatant enzyme preparations. A series of [35S]sulfate-containing substances, which closely resembled the homologous series of [35S]sulfate-labeled Triton X-100 oligomers formed by adrenal cortex enzymes, were formed in detergent-free adrenal incubates. Their chromatographic behavior suggests that they are not steroid sulfates. The kidney supernatant enzyme fraction was shown to contain steroid sulfotransferase activity; sulfation of cholesterol, dehydroepiandrosterone, pregnenolone, cholic acid and lithocholic acid was stimulated by the presence of Triton X-100.