Erratum to: Purification and characterization of iron-cofactored superoxide dismutase from Enteromorpha linza
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چکیده
منابع مشابه
Iron-responsive regulation of the Helicobacter pylori iron-cofactored superoxide dismutase SodB is mediated by Fur.
Maintaining iron homeostasis is a necessity for all living organisms, as free iron augments the generation of reactive oxygen species like superoxide anions, at the risk of subsequent lethal cellular damage. The iron-responsive regulator Fur controls iron metabolism in many bacteria, including the important human pathogen Helicobacter pylori, and thus is directly or indirectly involved in regul...
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Extracellular superoxide dismutase (EC-SOD) is the major isozyme of SOD in arteries, but is also abundant in lungs. In particular, mouse lungs contain large amounts of EC-SOD compared to lungs in other mammals. This suggests that EC-SOD may have an amplified function in the mouse lung. This study describes the purification and characterization of mouse EC-SOD as well as its localization in mous...
متن کاملPurification and characterization of an iron superoxide dismutase and a catalase from the sulfate-reducing bacterium Desulfovibrio gigas.
The iron-containing superoxide dismutase (FeSOD; EC 1.15.1.1) and catalase (EC 1.11.1.6) enzymes constitutively expressed by the strictly anaerobic bacterium Desulfovibrio gigas were purified and characterized. The FeSOD, isolated as a homodimer of 22-kDa subunits, has a specific activity of 1,900 U/mg and exhibits an electron paramagnetic resonance (EPR) spectrum characteristic of high-spin fe...
متن کاملPurification and properties of superoxide dismutase from Drosophila melanogaster.
The major superoxide dismutase ("slow" electromorph) of the fruit fly, Drosophila melanogaster, has been purified to homogeneity. This enzyme contains 2 Cu2+ and 2 Zn2+/molecule. The ultraviolet absorption spectrum indicates a lack of tryptophan. This enzyme has a molecular weight of 32,000 and is composed of two subunits of equal size, which are joined by noncovalent interactions. Cyanide at 1...
متن کاملThe purification and properties of superoxide dismutase from Neurospora crassa.
Soluble extracts of Neurospora crassa contain a single, electrophoretically distinct, superoxide dismutase. This enzyme has been isolated and has been found to be a bluegreen, copperand zinc-containing enzyme, similar to that already described from bovine tissues and from garden peas. The molecular weight was ,approximately 31,000, and the enzyme appeared to be composed of 2 subunits of equal s...
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ژورنال
عنوان ژورنال: Chinese Journal of Oceanology and Limnology
سال: 2014
ISSN: 0254-4059,1993-5005
DOI: 10.1007/s00343-014-0238-7