Abstract
1. 1. The purification (57% total recovery) of two arylsulphatases from the digestive juice of the snail Helix pomatia is described. 2. 2. Both sulphatases are free from β-glucuronidase and N-acetyl- β-glucosaminidase, and electrophoresis on acrylamide gels detects no protein other than that associated with the arylsulphatase activity. 3. 3. Gel isoelectric focussing shows five protein bands (pH 3.9–4.8), all associated with arylsulphatase activity, in both fractions. 4. 4. The arylsulphatases have a wide specificity, with considerable variation in K m and V, and are inhibited by sulphate and sulphite. 5. 5. The variation of K m, K i and V with pH is described: p K m varies linearly with pH between pH 5–9 (slope −1). 6. 6. The arylsulphatase and steroid sulphatase activities of the preparations are associated with a single protein.
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