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S9636

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Superoxide Dismutase from human erythrocytes

essentially salt-free, lyophilized powder, ≥2,500 units/mg protein

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Synonym(s):
SOD, Superoxide: superoxide oxidoreductase
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
NACRES:
NA.54

form

essentially salt-free, lyophilized powder

Quality Level

specific activity

≥2,500 units/mg protein

mol wt

32.0 kDa

composition

Protein, ≥80% biuret

technique(s)

activity assay: suitable

suitability

suitable for molecular biology

UniProt accession no.

storage temp.

−20°C

Gene Information

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This Item
S7446S7571S8160
specific activity

≥2,500 units/mg protein

specific activity

≥4,500 units/mg protein

specific activity

≥3,000 units/mg protein

specific activity

≥1500 units/mg protein

Gene Information

human ... SOD1(6647), SOD2(6648), SOD3(6649)

Gene Information

-

Gene Information

cow ... SOD1(281495), SOD2(281496)

Gene Information

cow ... SOD1(281495)

form

essentially salt-free, lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

mol wt

32.0 kDa

mol wt

32.5 kDa

mol wt

32.5 kDa

mol wt

32.5 kDa

Quality Level

400

Quality Level

200

Quality Level

300

Quality Level

200

General description

Superoxide dismutases (SOD) are a group of low molecular weight metalloproteins present in all aerobic cells of plants, animals and micro-organisms. Three forms of SOD exist, based on the metal ions in the active site. These are Cu2+/Zn2+, Mn2+ and Fe2+ containing SOD. In vertebrate organisms, Cu/Zn-SOD is located in the cytoplasm as well as the mitochondrial intermembrane space, whereas Mn-SOD is located at the mitochondrial matrix space in prokaryotes. Fe-SOD is also found in prokaryotes and higher plants. Human erythrocyte SOD is a non-covalently bound homodimeric protein with two 16.3 kDa subunits containing 153 amino acids. Each dimer consists of two Cu2+ atoms and two Zn2+ atoms.

Application

Superoxide Dismutase from human erythrocytes has been used:

  • to test its effect on human neutrophils in reactive oxygen species (ROS) measurement studies involving Pseudomonas aeruginosa infection
  • as an antioxidant to test its effect on ROS generation induced by atmospheric-pressure plasma jet (APPJ) in red blood cell (RBC) homogenates using optical spectroscopy studies
  • to test its attenuating effect on hemoglobin (Hb)-induced nuclear factor-kappa B (NF- κB) and hypoxia-inducible factor (HIF) activity in human dermal microvascular endothelial cells (HMECs-1)
  • as a reference antioxidant protein to examine its expression in human intestinal Caco-2 cells following treatment with dietary flavonoids
  • in combination with catalase to promote cell differentiation in vitro

Biochem/physiol Actions

Mutations in the SOD1 gene are implicated in Amyotrophic lateral sclerosis (ALS).
Catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. Plays a critical role in the defense of cells against the toxic effects of oxygen radicals. Competes with nitric oxide (NO) for superoxide anion (which reacts with NO to form peroxynitrite), thereby SOD promotes the activity of NO. SOD has also been shown to suppress apoptosis in cultured rat ovarian follicles, neural cell lines, and transgenic mice.

Unit Definition

One unit will inhibit reduction of cytochrome c by 50% in a coupled system with xanthine oxidase at pH 7.8 at 25 °C in a 3.0 mL reaction volume. Xanthine oxidase concentration should produce an initial ΔA550 of 0.025 ± 0.005 per min.

Analysis Note

For assay method, see McCord, J.M. and Fridovich, I., J. Biol. Chem., 244, 6049 (1969).

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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L Guemouri et al.
Clinical chemistry, 37(11), 1932-1937 (1991-11-01)
We studied the biological variability of blood superoxide dismutase (SOD; EC 1.15.1.1), glutathione peroxidase (GPX; EC 1.11.1.9), and catalase (CAT; EC 1.11.1.6) in a sample of 1836 apparently health subjects, ages 4-97 years. SOD and GPX activities were assayed in
M Iu Eropkin et al.
Voprosy meditsinskoi khimii, 45(5), 384-388 (2000-01-15)
An oxidative stress is considered to be one of the major mechanisms of cytotoxicity. The purpose of present work was to study effects of some drugs with antihypoxic/antioxidant activity in cultured human lung embryonic fibroblasts under conditions of cytotoxic response
Christina Lisk et al.
American journal of respiratory cell and molecular biology, 49(4), 619-626 (2013-05-30)
The release of hemoglobin (Hb) with hemolysis causes vascular dysfunction. New evidence implicates Hb-induced NF-κB and hypoxia inducible factor (HIF) activation, which may be under the control of a Toll-like receptor (TLR)-signaling pathway. Nearly all TLR-signaling pathways activate the myeloid
J V Bannister et al.
CRC critical reviews in biochemistry, 22(2), 111-180 (1987-01-01)
The current status of superoxide dismutase (SOD) is that it is an enzyme with diverse ramifications. This review attempts an understanding of SOD as a structural, functional, and biological entity. Accordingly, the review is in three parts. The first part
Expression of antioxidant proteins in human intestinal Caco-2 cells treated with dietary flavonoids
S Kameoka, et al.
Cancer Letters, 146(2), 161-167 (1999)

Articles

Oxidative stress is mediated, in part, by reactive oxygen species produced by multiple cellular processes and controlled by cellular antioxidant mechanisms such as enzymatic scavengers or antioxidant modulators. Free radicals, such as reactive oxygen species, cause cellular damage via cellular.

Protocols

Enzymatic Assay of Superoxide Dismutase

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