Distinctive properties of the catalase B of Aspergillus nidulans

被引：21

作者：

Calera, JA ^{[1
]}

Sánchez-Weatherby, J ^{[1
]}

López-Medrano, R ^{[1
]}

Leal, F ^{[1
]}

机构：

[1] Univ Salamanca, Dept Genet & Microbiol, Edificio Dept Biol, Lab 218, Salamanca 37007, Spain

来源：

FEBS LETTERS | 2000年 / 475卷 / 02期

关键词：

catalase; 3-aminotriazole; hydroperoxidase; Aspergillus nidulans;

D O I：

10.1016/S0014-5793(00)01637-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：117 / 120

页数：4

共 25 条

[1]

AEBI H, 1984, METHOD ENZYMOL, V105, P121

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