来自嗜树栖短杆菌AZ菌株的含铁超氧化物歧化酶的纯化与特性分析
Purification and characterization of Fe-containing superoxide dismutase from Methanobrevibacter arboriphilus strain AZ.
作者信息
Brioukhanov A L, Nesatyy V J, Netrusov A I
机构信息
Department of Microbiology, Faculty of Biology, Lomonosov Moscow State University, 119992 Moscow, Russia.
出版信息
Biochemistry (Mosc). 2006 Apr;71(4):441-7. doi: 10.1134/s0006297906040134.
Superoxide dismutase (SOD) was purified from cells of the strict anaerobic methanogenic archaeon Methanobrevibacter arboriphilus strain AZ. The four-step purification procedure resulted in enzyme with specific activity of 3970 units/mg and yield of 22%. It was shown that the SOD is a Fe-containing homotetramer composed of subunits of 21.2 kD each. Sodium azide (13.5 mM), unlike KCN, inhibits the activity of the SOD. Hydrogen peroxide (0.5 mM) inactivates the enzyme, which is consistent with the properties of the known Fe-containing SODs from methanogenic Archaea.
超氧化物歧化酶（SOD）是从严格厌氧的产甲烷古菌嗜树栖短杆菌AZ菌株的细胞中纯化得到的。四步纯化程序得到的酶比活性为3970单位/毫克，产率为22%。结果表明，该SOD是一种含铁的同四聚体，每个亚基的分子量为21.2 kD。与氰化钾不同，叠氮化钠（13.5 mM）可抑制SOD的活性。过氧化氢（0.5 mM）可使该酶失活，这与已知的产甲烷古菌含铁SOD的特性一致。
Zotero 插件