Iron- and manganese-containing superoxide dismutases from Methylomonas J: identity of the protein moiety and amino acid sequence.
Iron- and manganese-containing superoxide dismutases from Methylomonas J: identity of the protein moiety and amino acid sequence.
复制标题
来自甲基单胞菌 J 的含铁和锰的超氧化物歧化酶：蛋白质部分和氨基酸序列的同一性。
作者：
T. Matsumoto;K. Terauchi;T. Isobe;K. Matsuoka;F. Yamakura
Mn-超氧化物歧化酶 (SOD) 和 Fe-SOD 是从甲基单胞菌 J 中分离出来的，甲基单胞菌是一种需氧甲基营养菌，分别在含有锰（富锰培养基）或铁（富铁培养基）的甲胺培养基中生长。 Mn-SOD的比活力为2250单位mg-1（mol of Mn）-1（mol二聚体）-1，酶的金属含量为每摩尔二聚体0.98 mol Mn和0.12 mol Fe，而Fe-SOD的金属含量为88.5单位mg-1（mol of Fe）-1（mol二聚体）-1和1.04 mol Fe和1.04 mol Fe。 0.02摩尔锰。在十二烷基硫酸钠存在下，无论有或没有尿素，电泳迁移率以及使用十八烷基硅酸盐柱和凝胶渗透柱的 HPLC 柱上的色谱行为是相同的。两种 SOD 的氨基酸组成几乎没有区别。通过用硫酸锰或硫酸亚铁铵透析从Mn酶获得的脱辅基蛋白，酶活性分别恢复到与天然Mn-SOD和天然Fe-SOD相似的活性水平。使用从 Fe 酶获得的脱辅基蛋白进行重建也报告了相同的结果 [Yamakura, F., Matsumoto, T., & Terauchi, K. (1990) Free Radical Res. (Yamakura, F., Matsumoto, T., & Terauchi, K. (1990) Free Radical Res.)交流。 （正在印刷中）]。这些结果表明，两种类型的 SOD 都可能由在富铁培养基或富锰培养基中生长的细胞中合成的单一脱辅基蛋白组成。（摘要截断为 250 字）
Mn-superoxide dismutase (SOD) and Fe-SOD were isolated from Methylomonas J, an aerobic methylotrophic bacterium, grown in methylamine media containing either manganese (Mn-rich medium) or iron (Fe-rich medium), respectively. The specific activity of the Mn-SOD was 2250 units mg-1 (mol of Mn)-1 (mol of dimer)-1, and the metal content of the enzyme was 0.98 mol of Mn and 0.12 mol of Fe per mole of dimer, while those of Fe-SOD were 88.5 units mg-1 (mol of Fe)-1 (mol of dimer)-1 and 1.04 mol of Fe and 0.02 mol of Mn. The electrophoretic mobilities in the presence of sodium dodecyl sulfate, with or without urea, and the chromatographic behavior on an HPLC column using an octadodecyl silicated column and a gel permeation column were identical. Amino acid compositions were practically indistinguishable in both SODs. The enzyme activity was restored by dialysis of an apoprotein obtained from the Mn-enzyme with either manganese sulfate or ferrous ammonium sulfate up to an activity level similar to that for the native Mn-SOD and the native Fe-SOD, respectively. The same result has been reported with the reconstitution using an apoprotein obtained from the Fe-enzyme [Yamakura, F., Matsumoto, T., & Terauchi, K. (1990) Free Radical Res. Commun. (in press)]. These results suggest the possibility that both types of SODs are composed of a single apoprotein synthesized in cells grown in either the Fe-rich medium or the Mn-rich medium.(ABSTRACT TRUNCATED AT 250 WORDS)
从脆弱拟杆菌中分离含铁超氧化物歧化酶：重构为含锰酶。
影响因子：
3.9
作者：
Gregory,EM;Dapper,CH
通讯作者：
Dapper,CH