Abstract
1. 1. Arylsulphatase in Proteus rettgeri was separated into four fractions by DEAE-cellulose chromatography. 2. 2. Fractions 2, 3 and 4 were shown by polyacrylamide-gel electrophoresis and/or sucrose density gradient centrifugation to contain more than one form of the enzyme. Some forms differed in substrate specificity. 3. 3. Arylsulphatase present in fraction 1 was previously shown to be homogeneous by paper electrophoresis and some properties of this enzyme have been determined. These include a substratedependent activation by PO 4 3− and a shift in optimum pH in the presence of CN −.
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