Journal
FEBS LETTERS
Volume 475, Issue 2, Pages 117-120Publisher
WILEY
DOI: 10.1016/S0014-5793(00)01637-9
Keywords
catalase; 3-aminotriazole; hydroperoxidase; Aspergillus nidulans
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Aspergillus nidulans catalase B (CatB) was purified to homogeneity and characterized as a hydroperoxidase which resembles typical catalases in some physicochemical characteristics: (1) it has an apparent molecular weight of 360 000 and is composed of four glycosylated subunits, (2) it has hydrophobic properties as revealed by extractability in ethanol/chloroform and binding to phenyl-Superose, and (3) it has an acidic isoelectric point at pH 3.5. Also CatB exhibits some distinctive properties, e.g. it is not inhibited by the presence of 2% sodium dodecyl sulfate, 9 M urea or reducing agents. Furthermore, even though CatB does not exhibit any residual peroxidase activity, it is able to retain up to 38% of its initial catalase activity after incubation with the typical catalase inhibitor 3-amino-1,2,4-triazole, (C) 2000 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
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