Tolfo Bittencourt Sílvia Elena, Amaral de Castro Luiza, Estrazulas Farias Sandra, Nair Bao Sônia, Schrank Augusto, Henning Vainstein Marilene
Departamento de Biologia Celular, Instituto de Ciências Biológicas, Universidade de Brasília, Brasília, Brazil.
Res Microbiol. 2004 Oct;155(8):681-7. doi: 10.1016/j.resmic.2004.04.012.
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.
昆虫病原真菌绿僵菌含有三种超氧化物歧化酶。其中一种酶被纯化并部分鉴定为铜锌超氧化物歧化酶。该酶的估计分子量为30690 Da，比活性为3838.89 Umg(-1)。SDS-PAGE和二维凝胶显示，从凝胶过滤柱洗脱的组分中分别有一条分子量为20000和大约15000 Da的单一蛋白条带，pI为6.0。这些结果表明天然酶是由两个亚基组成的二聚体。制备了针对纯化的铜锌超氧化物歧化酶的多克隆抗血清，并通过免疫电子显微镜确定其亚细胞定位。绿僵菌铜锌超氧化物歧化酶存在于细胞壁中。
