Purification and ultrastructural localization of a copper-zinc superoxide dismutase (CuZnSOD) from the entomopathogenic and acaricide fungus Metarhizium anisophae

被引：11
作者：
Bittencourt, SET
de Castro, LA
Farias, SE
Bao, SN
Schrank, A
Vainstein, MH
机构：
[1] Univ Fed Rio Grande do Sul, Ctr Biotechnol, BR-90540000 Porto Alegre, RS, Brazil
[2] Univ Brasilia, Inst Ciencias Biol, Dept Biol Celular, Brasilia, DF, Brazil
[3] Univ Fed Rio Grande do Sul, Inst Ciencias Basicas Saude, Dept Fisiol, Porto Alegre, RS, Brazil
[4] Univ Fed Rio Grande do Sul, Inst Biociencias, Dept Mol Biol & Biotechnol, BR-90049 Porto Alegre, RS, Brazil
[5] Univ Fed Rio Grande do Sul, Inst Ciencias Basicas Saude, Dept Microbiol, BR-90049 Porto Alegre, RS, Brazil
来源：
RESEARCH IN MICROBIOLOGY | 2004年 / 155卷 / 08期
关键词：
Metarhizium anisopliae; superoxide dismutase (SOD); antioxidant enzyme; active oxygen species (AOS); oxygen free radicals (OFR); biological control;
D O I：
10.1016/j.resmic.2004.04.012
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
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 20 000 and similar to 15 000 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. (C) 2004 Elsevier SAS. All rights reserved.
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页码：681 / 687
页数：7
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