Apte, B. N. ; Siddiqi, O. (1971) Purification and properties of arylsulphatase of Aspergillus nidulans Biochimica et Biophysica Acta (BBA) - Enzymology, 242 (1). pp. 129-140. ISSN 0005-2744
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Official URL: http://www.sciencedirect.com/science/article/pii/0...
Related URL: http://dx.doi.org/10.1016/0005-2744(71)90094-5
Abstract
A method for the purification of arylsulphatase (aryl-sulphate sulphohydrolase, EC 3.1.6.1) of Aspergillus nidulans has been described. The enzyme elutes from DEAE-cellulose in two distinct fractions, designated as Fraction I and Fraction II. Fraction I was purified over 450-fold and Fraction II over 600-fold. The two fractions were characterized with respect to some of their physical and biochemical properties. They differ in their Km values for p-nitrophenyl sulphate and nitrocatechol sulphate, sensitivity to some inhibitors, electrophoretic mobility and heat stability. In most other properties they are similar.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to Elsevier Science. |
| ID Code: | 52794 |
| Deposited On: | 04 Aug 2011 08:35 |
| Last Modified: | 04 Aug 2011 08:35 |
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