Purification and Some Properties of Human Liver Iduronate Sulfatase1

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Abstract
Iduronate sulfatase was purified from human liver for an investigation of the degra-dative pathway of dermatan sulfate. An overall 80-fold purification was achieved and, more importantly, the preparation was free of α-L-iduronidase, β-glucuronidase, N -acetylgalactosamine 4-sulfate sulfatase (arylsulfatase B) and highly enriched in β- N -acetylhexosaminidase. The liver enzyme appeared to be composed of several molecular species. The enzyme activity was optimal at pH 4.0 and its K m was 10–20 µm with sulfoiduronyl sulfoanhydromannitol. Chloride was inhibitory at high concentration and among divalent metal ions, only copper was inhibitory. Nitro-catechol sulfate was not a substrate, but did show competitive inhibition. Its K 1 for iduronate sulfatase was similar to its K m for arylsulfatase, suggesting a similarity in the substrate binding sites of iduronate sulfatase and arylsulfatases.

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