Superoxide dismutase activity of Mycobacterium avium, M. intracellulare, and M. scrofulaceum.
Superoxide dismutase activity of Mycobacterium avium, M. intracellulare, and M. scrofulaceum.
复制标题
鸟分枝杆菌、胞内分枝杆菌和瘰疬分枝杆菌的超氧化物歧化酶活性。
DOI：
10.1128/iai.53.3.631-635.1986
复制
发表时间：
1986
影响因子：
3.1
通讯作者：
Falkinham3rd,JO
中科院分区：
文献类型：
--
作者：
Mayer,BK;Falkinham3rd,JO
对鸟分枝杆菌（Mycobacterium avium）、胞内分枝杆菌（M.胞内分枝杆菌）和结核分枝杆菌（M. scrofulaceum， MAIS） 3种典型菌株的细胞粗提物进行了超氧化物歧化酶（SOD）活性检测。聚丙烯酰胺凝胶电泳显示，尽管MAIS菌株的迁移率存在差异，但每种菌株都具有单一的SOD活性带。所有禽分枝杆菌和胞内分枝杆菌以及5株结核分枝杆菌中2株结核分枝杆菌的SOD活性条带迁移率相同（Rf = 0.83），其余3株结核分枝杆菌的SOD活性条带迁移距离更远（Rf = 0.85）。迁移率的差异与对NaN3和H2O2的敏感性差异相关。在5 mM H2O2作用15 min后，大多数具有较慢迁移活性带的MAIS菌株的SOD活性被抑制了22% ~ 81%，表明铁和锰可能同时存在于一个酶中。3株具有快速迁移活性带的M. scrofulaceum菌株的SOD活性在5 mM H2O2作用5 min后被100%抑制，对5和10 mM NaN3的敏感性更高，具有含铁SOD的特征。1 mM KCN浓度对MAIS菌株的酶活性均无抑制作用。在6株MAIS菌株中检测到4株细胞外SOD活性，其活性与粗提取物的活性相同。
Superoxide dismutase (EC 1.15.1.1) (SOD) activity has been detected in crude cell extracts of representative strains of the Mycobacterium avium, M. intracellulare, and M. scrofulaceum (MAIS) group. Polyacrylamide gel electrophoresis demonstrated a single SOD activity band for each of the MAIS strains, though there were differences in mobility. All M. avium and M. intracellulare and two of five M. scrofulaceum strains demonstrated a single activity band of identical mobility (Rf = 0.83), while the SOD activity band for the three remaining M. scrofulaceum strains migrated farther (Rf = 0.85). The differences in mobility correlated with differences in sensitivity to NaN3 and H2O2. The SOD activities of the majority of the MAIS strains which displayed the slower-migrating activity band were inhibited 22 to 81% after 15 min of exposure to 5 mM H2O2, suggesting that both iron and manganese may be present in a single enzyme. The SOD activities of the three M. scrofulaceum strains which had the faster-migrating activity band were inhibited 100% after only 5 min of exposure to 5 mM H2O2 and exhibited greater sensitivity to 5 and 10 mM NaN3, characteristics of an iron-containing SOD. A concentration of 1 mM KCN did not cause inhibition of enzyme activity in any of the MAIS strains tested. Extracellular SOD activity was detected in four of six MAIS strains and was shown to be identical in mobility to the SOD activity of the crude extracts.