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Copper-zinc superoxide dismutase from the marine yeast Debaryomyceshansenii

机译:海洋酵母Debaryomyceshansenii中的铜锌超氧化物歧化酶

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摘要

We have isolated the cytosolic form of Cu-Zn superoxide dismutase (SOD) from the marine yeast Debaryomyces hansenii. This enzyme has a subunit mass of 18 kDa. The preparation was found to be heterogeneous by IF electrophoresis with two pI ranges: 5.14-4.0 and 1.6-1.8. The enzyme preparation had a remarkably strong stability at pH 6.0-7.0, surviving boiling for 10 min without losing more than 60% of activity. On Western blots, this enzyme was recognized by antibodies raised in rabbits against D. hansenii extracts, while only a weak cross-reaction could be detected using antibodies generated against either Saccharomyces cerevisiae or bovine erythrocyte Cu-Zn SODs. In sequencing analysis, a peptide obtained by trypsin digestion was found to have 85% identity to the S. cerevisiae Cu-Zn SOD. Copyright (C) 1999 John Wiley & Sons, Ltd.
机译:我们已经从海洋酵母汉逊德巴利酵母分离出了铜锌超氧化物歧化酶(SOD)的胞质形式。该酶的亚基质量为18 kDa。通过IF电泳发现该制剂是异质的,具有两个pI范围:5.14-4.0和1.6-1.8。该酶制剂在pH 6.0-7.0时具有非常强的稳定性,可以在沸腾10分钟后存活,而不会损失超过60%的活性。在Western印迹上,该酶被兔抗汉逊酵母提取物产生的抗体识别,而使用酿酒酵母或牛红细胞Cu-Zn SOD产生的抗体只能检测到较弱的交叉反应。在测序分析中,发现通过胰蛋白酶消化获得的肽与酿酒酵母Cu-Zn SOD具有85%的同一性。版权所有(C)1999 John Wiley&Sons,Ltd.

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