Abstract
A method is described for the purification and assay of the sulfatase C of ox liver, an extremely insoluble enzyme which has not been obtained in solution. Its properties are described. The optimum conditions for the assay of sulfatase C are a substrate concentration of 0.01 [image] p-nitrophenyl sulfate at pH 8.0. Sulfatase C hydrolyzes nitrocatechol sulfate at approximately half the rate of p-nitrophenyl sulfate. It is inhibited by Na+ ions and to a lesser extent by K+ ions. A number of other inhibitors were studied and it is concluded that sulfatase C is an SH enzyme. The properties are compared with those of other aryl sulfatases. The problem of assaying sulfatases in unfractionated-tissue preparations is discussed.