Tetrameric manganese superoxide dismutases from anaerobic Actinomyces.
Tetrameric manganese superoxide dismutases from anaerobic Actinomyces.
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来自厌氧放线菌的四聚体锰超氧化物歧化酶。
DOI：
10.1016/0003-9861(90)90535-7
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发表时间：
1990
影响因子：
3.9
通讯作者：
Gregory,EM
中科院分区：
文献类型：
--
作者：
Barkley,KB;Gregory,EM
超氧化物歧化酶分离自厌氧生长的生物体内氏放线菌、放线菌菌株E1S.25D和溶牙放线菌。该酶为100，000 - 110，000 mol wt酸性蛋白质（pI4.3-4.6），含有Mn和Zn，但未检测到Fe。Mn、Zn含量因酶源不同而异。Naeslundii超氧化物歧化酶比活力2200 U/mg，每摩尔四聚体含Mn 2.3 g，Zn 1.4 g。溶齿菌SOD比活700 U/ mg，每摩尔四聚体含锰1.4 g，锌1.8 g，放线菌E1S.25D比活1300 U/mg，每摩尔四聚体含锰1.8 g，锌1.2 g。除了精氨酸、赖氨酸和色氨酸含量外，酶的氨基酸组成相当。各酶在5 mmH_2O_2中23 °C作用2 h，酶活稳定。20 mmNaN 3仅适度抑制酶。酶活性增加，在低离子强度，但显着降低，在增加的离子强度与除高氯酸钠，这导致显着的抑制，即使在低离子强度测试的每种盐。抗A. Naeslundii和放线菌菌株E1S.25D沉淀并灭活各自的抗原，而沉淀的A. odontolyticus超氧化物歧化酶-抗体复合物保留了几乎全部的催化活性。免疫学研究表明，nativeA.内氏菌和放线菌E1S.25D MnSODs具有共同的抗原决定簇，在Ouchterlony双扩散凝胶中与完全相同的沉淀素线发生交叉反应。抗A.溶牙菌酶与另外两种放线菌的超氧化物歧化酶仅表现出部分交叉反应。变性抗原的Western印迹显示抗体的反应性，其与Ouchterlony凝胶的结果仅略有不同。
Superoxide dismutase was isolated from each of the anaerobically grown organismsActinomyces naeslundii, Actinomycesstrain E1S.25D, andActinomyces odontolyticus. The enzymes were 100,000–110,000 mol wt acidic proteins (pI4.3–4.6) and contained Mn and Zn, but no detectable Fe. The Mn and Zn content varied with the enzyme source.A. naeslundiisuperoxide dismutase, specific activity 2200 U/mg, contained 2.3 g atoms Mn and 1.4 g atoms Zn per mole tetramer whereasA. odontolyticusSOD, specific activity 700 U/ mg, contained 1.4 g atoms Mn and 1.8 g atoms Zn per mole tetramer.Actinomycesstrain E1S.25D, specific activity 1300 U/mg, contained 1.8 g atoms Mn and 1.2 g atoms Zn per mole tetramer. The amino acid compositions of the enzymes were comparable except for arginine, lysine, and tryptophan content. The enzymatic activity of each enzyme was stable in 5 mmH2O2at 23 °C for 2 h. The enzymes were only modestly inhibited by 20 mmNaN3. The enzymatic activity was increased at low ionic strength but was markedly decreased at increased ionic strength with each salt tested except sodium perchlorate, which caused marked inhibition even at low ionic strength. Polyclonal antibodies toA. naeslundiiandActinomycesstrain E1S.25D precipitated and inactivated their respective antigens whereas the precipitatedA. odontolyticussuperoxide dismutase-antibody complex retained virtually full catalytic activity. Immunological studies revealed that the nativeA. naeslundiiandActinomycesstrain E1S.25D MnSODs share common epitopes and cross-reacted with precipitin lines of complete identity in Ouchterlony double diffusion gels. Antibody to theA. odontolyticusenzyme displayed only partial cross-reactivity with superoxide dismutase from the two otherActinomyces. Western blotting of the denatured antigens revealed reactivities of the antibodies that differed only slightly from the results of the Ouchterlony gels.
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嗜热栖热菌 HB8 超氧化物歧化酶的纯化和性质。
影响因子：
2.7
作者：
S. Sato;K. Nakazawa
通讯作者：
K. Nakazawa
影响因子：
3.9
作者：
HATCHIKIAN, EC;HENRY, YA
通讯作者：
HENRY, YA
影响因子：
7.4
作者：
M. Salin;S. Bridges
通讯作者：
M. Salin;S. Bridges
蛋白质、氨基酸和肽
DOI：
--
发表时间：
1943
期刊：
影响因子：
--
作者：
R. Oppermann
通讯作者：
R. Oppermann
来自真核生物银杏的含铁超氧化物歧化酶的纯化和表征。
影响因子：
3.9
作者：
Mary V. Duke;M. Salin
通讯作者：
M. Salin