Purification and ultrastructural localization of a copper-zinc superoxide dismutase (CuZnSOD) from the entomopathogenic and acaricide fungus Metarhizium anisopliae.
Res Microbiol
; 155(8): 681-7, 2004 Oct.
Article
em En
| MEDLINE
| ID: mdl-15380557
The entomopathogenic fungus Metarhizium anisopliae contains three superoxide dismutases. One of these enzymes was purified and partially characterized as a CuZnSOD. The enzyme has an estimated molecular mass of 30690 Da and a specific activity of 3838.89 Umg(-1). SDS-PAGE and 2D gels show a single band of protein in the fractions eluted from the gel filtration column with a molecular mass of 20000 and approximately 15000 Da, respectively, and a pI of 6.0. These results suggest that the native enzyme is a dimer consisting of two subunits. Polyclonal antiserum were raised against purified CuZnSOD and used to determine its subcellular localization by immunoelectron microscopy. M. anisopliae CuZnSOD is present in the cell wall.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Superóxido Dismutase
/
Cobre
/
Hypocreales
Idioma:
En
Revista:
Res Microbiol
Assunto da revista:
MICROBIOLOGIA
Ano de publicação:
2004
Tipo de documento:
Article
País de afiliação:
Brasil
País de publicação:
França