Abstract
Abstract— Arylsulphatases (aryl‐sulphate sulphohydrolases; E.C. 3.1.6.1) in the soluble subcellular fraction (105000g, 2 h) of human brain were partially purified by ammonium sulphate fractionation, ion exchange chromatography, and Sephadex gel filtration. Potassium‐4‐methylumbelliferone‐sulphatase (MUS‐sulphatase) adsorbed on DEAE‐cellulose was purified approximately 700‐fold over activity in the soluble fraction and the unadsorbed MUS‐sulphatase was similarly purified approximately 600‐fold. The arylsulphatase adsorbed to DEAE‐cellulose exhibited a Km value for MUS of 12.5 mM and a pH optimum of 5.7, whereas the unadsorbed arylsulphatase exhibited a Km value for MUS of 8.3 mM and a pH optimum of 5.4. The molecular weights of the two enzymes were approximately 109,600 and 51,300, respectively. Sulphate (0.5 mM) showed pronounced mixed inhibition only of the unadsorbed arylsulphatase. Ag+ ions (0.25 mM) showed 96 per cent inhibition of the adsorbed arylsulphatase, whereas an activation of the unadsorbed arylsulphatase was observed.

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