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. 1977 Jul 1;165(1):127-34.
doi: 10.1042/bj1650127.

Purification and some properties of arylsulphatases A and B from rabbit kidney cortex

J J Helwig, A A Farooqui, C Bollack, P Mandel

Purification and some properties of arylsulphatases A and B from rabbit kidney cortex

J J Helwig et al. Biochem J. .

Abstract

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.

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