Purification and some properties of arylsulphatases A and B from rabbit kidney cortex.
Arylsulphatases A and B (EC 3.1.6.1) of rabbit kidney cortex were purified 5250- and 7720-fold respectively by a multiple-column-chromatography method. The specific activity toward 4-nitrocatechol sulphate was 42mumol/min per mg  for arylsulphatase A and 62 mumol/min per mg for arylsulphatase B. Each enzyme migrated as a single band on polyacrylamide-gel electrophoresis, and the enzyme activity corresponded to the band of protein on the gel. The rate of hydrolysis of ascorbic acid 2-sulphate by arylsulphatase A was three times that for cerebroside 3-sulphate. Arylsulphatase B hydrolysed UDP-N--acetylgalactosamine 4-sulphate and glucosamine 4,6-disulphate, but not galactosamine 6-sulphate.
D000818:Animals; D002553:Cerebroside-Sulfatase / Q000302:isolation & purification; D055598:Chemical Phenomena; D002621:Chemistry; D002803:Chondro-4-Sulfatase / Q000302:isolation & purification; D002850:Chromatography, Gel; D007672:Kidney Cortex / Q000201:enzymology*; D007700:Kinetics; D011817:Rabbits; D013429:Sulfatases / Q000302:isolation & purification
D013429:Sulfatases; D002553:Cerebroside-Sulfatase; D002803:Chondro-4-Sulfatase