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News Release from: Genaxxon Bioscience | Subject: Sods
Edited by the Laboratorytalk Editorial
Team on 21 November 2003
Superoxide dismutases for neuroscience
research
Superoxide dismutases (Sods) catalyse the disproportionation of superoxide anion radicals to yield molecular oxygen and hydrogen peroxide
Superoxide dismutases (Sods; EC 1.15.1.1) belong to a family of metalloenzymes which catalyse the disproportionation of superoxide anion (O2-) radicals to yield molecular oxygen and hydrogen peroxide (H2O2) Superoxide dismutases (Sods) catalyse the proton-dependent dismutation of two superoxide radical anions to molecular oxygen and hydrogen peroxide
This article was originally published on Laboratorytalk on 20 Nov 2003 at 8.00am (UK)
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The biological functions of Sods are very important because they prevent oxidative damage and inflammation, due to subsequent formation of oxygen intermediates derived from the superoxide, and are involved in anticancer and antiaging mechanisms.
Cu/Zn Sod plays a protective role in the pathogenesis of selective neuronal injury after brief ischemia and reduces the degree of necrotic and DNA fragmented neuronal death following global ischemia.
The main function of Sod is to scavenge O2- radicals generated in various physiological processes, thus preventing the oxidation of biological molecules, either by the radicals themselves, or by their derivatives.
A number of environmental stresses can lead to enhanced production of O2- within plant tissues, and plants are believed to rely on the enzyme SOD to detoxify this reactive oxygen species.
1-3 copper zinc superoxide dismutase, Cu/Zn Sod, is a dimeric protein with two identical subunits bonded noncovalently.
Each subunit contains one copper(II) and one zinc(II) ion in the oxidised state of the metalloenzyme.
During catalysis, copper is the redox partner of the superoxide radical.
Genaxxon has access to the first commercial source for this important protein in its recombinant human origin.
The Sod is expressed in E coli and equalls the human Cu/Zn Sod.
The molecular weigth of this hrSod is 17 kDa.
The purity of the delivered enzyme is >90% (by SDS-Page).
Since it is a recombinant protein you don't have to deal with potentially biohazardous material of human origin.
With the availability of Cu/Zn Sod in larger quantaties research groups can launch new approaches towards the investigation of functional ways of oxidative stress, neurodegenerative diseases (such as amyotrophic lateral sclerosis) and celluar ageing.
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