Arylsulphatases A and B (EC 184.108.40.206) 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.
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Research Article| July 01 1977
Purification and some properties of arylsulphatases A and B from rabbit kidney cortex
A A Farooqui;
Biochem J (1977) 165 (1): 127–134.
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J J Helwig, A A Farooqui, C Bollack, P Mandel; Purification and some properties of arylsulphatases A and B from rabbit kidney cortex. Biochem J 1 July 1977; 165 (1): 127–134. doi: https://doi.org/10.1042/bj1650127
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