ISOLATION AND CHARACTERIZATION OF THE IRON-CONTAINING SUPEROXIDE-DISMUTASE OF METHANOBACTERIUM-BRYANTII
ISOLATION AND CHARACTERIZATION OF THE IRON-CONTAINING SUPEROXIDE-DISMUTASE OF METHANOBACTERIUM-BRYANTII
复制标题
DOI：
10.1016/0003-9861(81)90174-0
复制
发表时间：
1981-01-01
影响因子：
3.9
通讯作者：
FRIDOVICH, I
中科院分区：
文献类型：
--
作者：
KIRBY, TW;LANCASTER, JR;FRIDOVICH, I
M. Bryantii含有单一的酶可识别的超氧化物歧化酶，其占可提取蛋白质的0.4%。该酶被纯化至电泳和超电泳均一性。看起来是四聚体。这些亚基是牢固的，但非共价键合，大小相同。该酶的分子量为91，000 ±。2000.该酶的比活性与先前提到的来自大肠杆菌的相应酶的比活性相同。该酶含有2.7个原子的Fe，1.7个原子的Zn，和< 0.2个原子的Mn/四聚体。其氨基酸组成将这种酶与其他含Mn和Fe的超氧化物歧化酶。分枝bryantii酶在其光学和EPR光谱以及其对H2 O2灭活的敏感性方面也类似于先前描述的含Fe超氧化物歧化酶。分枝Bryantii酶被N3-抑制，但对这种抑制剂的敏感性低于其他含铁超氧化物歧化酶。
M. bryantii contains a single electrophoretically discernible superoxide dismutase, which constitutes 0.4% of the extractable protein. This enzyme was purified to electrophoretic and ultracentrifugal homogeneity. It appears to be a tetramer. The subunits were tenaciously, but noncovalently bonded and were of identical size. The MW of the enzyme was 91,000 .+-. 2000. The specific activity of this enzyme was identical to that previously noted for the corresponding enzyme from Escherichia coli. The enzyme contained 2.7 atoms of Fe, 1.7 atoms of Zn, and < 0.2 atoms Mn per tetramer. Its amino acid composition placed this enzyme with the other Mn- and Fe-containing superoxide dismutases. The M. bryantii enzyme was also similar to previously described Fe-containing superoxide dismutases in its optical and EPR spectra and in its susceptibility to inactivation by H2O2. The M. bryantii enzyme was inhibited by N3-, but was less sensitive towards this inhibitor than other Fe-containing superoxide dismutases.