Isolation, purification and some properties of copper/zine superoxide dismutase in silkworm

Superoxide dismutase is an important antioxidant enzyme in animals and plays an important role to remove excess free radicals which achieved mainly through the copper-zinc superoxide dismutase and manganese superoxide dismutase. Copper may directly or indirectly affect the copper-zinc superoxide dismutase activity, while the change of reactive oxygen species induced by copper deficiency may regulate manganese superoxide dismutase expression through the transcription factor NF-κB and AP-1.

Dismutase

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Purification and Characterization of Superoxide Dismutase fromAerobacter aerogenes

Agricultural and Biological Chemistry (1991)

Si Wan Kim Sang Ok Lee Tae Ho Lee

Superoxide dismutase (SOD) was purified from Aerobacter aerogenes IFO 3317 to an electrophoretically homogeneous state and partially characterized. SOD was purified by ammonium sulfate fractionation, column chromatography on DEAE-Sephadex A-50, gel filtration on Sephadex G-100, phenyl-Toyopearl 650 M hydrophobic chromatography, and hydroxyapatite adsorption chromatography. The molecular weight and subunit molecular weight of the purified enzyme were estimated to be 45,000 and 22,000, respectively. The isoelectric point of the enzyme was about pH 4.0. The purified enzyme remained stable at pH 7.0–11.0, 25°C for 36hrs, but was rapidly inactivated below pH 7.0. SOD was stable up to 35°C at pH 7.0, but was inactivated at temperatures above that. The absorption maximum in the visible range was found at 360 nm, and the enzyme was insensitive to cyanide and fluoride, and sensitive to hydrogen peroxide and azide. These results suggest that the enzyme is an iron-containing SOD. The amino acid composition and the N-terminal sequence of the first 15 amino acids of the enzyme exhibited close homology with the other iron-containing SODs.

Sephadex

10.1080/00021369.1991.10870561

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Screening and Purification of Superoxide Dismutase Producing Marine Bacterium Using Phtochemically Generated Superoxide Ion

Korean Journal of Microbiology (2002)

조기웅

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A cupro-zinc protein with superoxide dismutase activity from horse liver. Isolation and properties

Comparative Biochemistry and Physiology Part B Comparative Biochemistry (1974)

V. Albergoni A. Cassini

Isolation

10.1016/0305-0491(74)90022-4

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Nickel-containing superoxide dismutase

Methods in enzymology on CD-ROM/Methods in enzymology (2002)

Jin‐Won Lee Jung‐Hye Roe Sa-Ouk Kang

Efflux

10.1016/s0076-6879(02)49324-x

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Expression, purification and molecular modeling of iron-containing superoxide dismutase from Acidithiobacillusferrooxidans

中国有色金属学会会刊：英文版 (2008)

刘元东高建邱冠周刘学瑞张成桂

从 Acidithiobacillus ferrooxidans 的 superoxide dismutase (草皮) 可以在它的忍耐起一个重要作用到 bioleaching 的极其有毒、氧化的环境。这基因在 Escherichia 被克隆然后成功地表示了 coli。表示蛋白质被一步舞亲密关系层析最后净化到同质并且观察了根据 SDS 页和 MALDI-TOF-MS 更暗淡。金属内容决心和 recombinant 蛋白质的光系列结果证实蛋白质是包含铁的 superoxide dismutase。为蛋白质的分子的建模表明铁原子被 His26， His75， Asp158 和 His162 绑扎。

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The enzyme copper/zinc-superoxide dismutase distribution in the human skin

Giovanna Giuseppina Altobelli Susan Van Noorden Marcello Marotta Claudia Rosati Vincenzo Cimini

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Expression, purification and characterisation of human copper-zinc superoxide dismutase protein and human-escherichia coli copper-zinc superoxide dismutase chimeric protein

Justine May Grixti Claude Farrugia Gary J. Hunter Thérèse Hunter

Dismutase

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