Hakamada Y, Koike K, Kobayashi T, Ito S
Tochigi Research Laboratories of Kao Corporation, Haga, Japan.
Extremophiles. 1997 May;1(2):74-8. doi: 10.1007/s007920050017.
A mangano-superoxide dismutase (EC 1.15.1.1) was purified to homogeneity from a strain of alkaliphilic Bacillus for the first time. The purified protein, with an isoelectric point of pH 4.5, had a molecular mass of approximately 50 kDa and consisted of two identical subunits (25 kDa). The N-terminal amino acid sequence was Ala-Tyr-Lys-Leu-Pro-Glu-Leu-Pro-Tyr-Ala-Ala-Asn-Ala-Leu-Glu-Pro-His-Ile- Asp-Glu-Ala. The optimum pH and temperature for the reaction were 7.5 and 35 degrees C, respectively. The properties of the superoxide dismutase were compared with those of the enzyme from thermophilic Bacillus stearothermophilus.
首次从一株嗜碱芽孢杆菌中纯化出了锰超氧化物歧化酶（EC 1.15.1.1），使其达到了同质状态。纯化后的蛋白质等电点为pH 4.5，分子量约为50 kDa，由两个相同的亚基（25 kDa）组成。其N端氨基酸序列为Ala-Tyr-Lys-Leu-Pro-Glu-Leu-Pro-Tyr-Ala-Ala-Asn-Ala-Leu-Glu-Pro-His-Ile-Asp-Glu-Ala。该反应的最适pH和温度分别为7.5和35摄氏度。将该超氧化物歧化酶的特性与嗜热脂肪芽孢杆菌的酶的特性进行了比较。
