Cytosolic sulfotransferase (SULT) SULT2B1b had previously been charac-terized as a cholesterol sulfotransferase. Like human SULT2B1, mouse SULT2B1b contains a unique, 31 amino acid C-terminal sequence with a proline⁄serine-rich region, which is not found in members of other SULT families. To gain insight into the functional relevance of this proline⁄ser-ine-rich region, we constructed a truncated mouse SULT2B1b lacking the 31 C-terminal amino acids, and compared it with the wild-type enzyme.
