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FEBS Lett. 2000 Jun 16;475(2):117-20.

Distinctive properties of the catalase B of Aspergillus nidulans.

Author information

1
Departamento de Microbiología y Genética, Universidad de Salamanca, Salamanca, Spain.

Abstract

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 360000 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.

PMID:
10858500
DOI:
10.1016/s0014-5793(00)01637-9
[Indexed for MEDLINE]
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