Distinctive properties of the catalase B of Aspergillus nidulans

FEBS Letters

López-Medrano, Ramiro¹  Sánchez-Weatherby, Juan¹  Leal, Fernando¹  Calera, José A¹ 

[1] Departamento de Microbiologı́a y Genética, Edificio Departamental de Biologı́a Laboratorio 218, Universidad de Salamanca, Pza. de los Doctores de la Reina s/n, 37007 Salamanca, Spain

关键词: Catalase;    3-Aminotriazole;    Hydroperoxidase;    Aspergillus nidulans;   

DOI  :  10.1016/S0014-5793(00)01637-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown