The preparation of the enzyme iduronate sulfatase from human placenta has been undertaken. The substrate O-(alpha-L-idopyranosyluronic acid 2-sulfate) (1 leads to 4)-2,5-anhydro-D-[3H]mannitol 6-sulfate was used to measure the enzymatic activity. The enzyme shows a pH optimum of 4.0 in 0.1 M sodium formiate or acetate buffer. Chromatography on DE-52 gives a 5.4 fold purification. The enzyme is inhibited by NaCl or KCl: in 20 mM salt the reaction rate was only 63% and 34% respectively. Inhibition by salt can be removed by extensive dialysis after the chromatographic step.