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S7571

Sigma-Aldrich

Superoxide Dismutase from bovine erythrocytes

greener alternative

lyophilized powder, ≥3,000 units/mg protein, Protein ≥95 % by biuret

Synonym(s):

CU/ZN-SOD, Superoxide Dismutase 1 bovine, cytocuprein, erythrocuprein, hemocuprein, SOD, Superoxide: superoxide oxidoreductase

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About This Item

CAS Number:
9054-89-1
Enzyme Commission number:
1.15.1.1 (BRENDA, IUBMB)
EC Number:
232-943-0
MDL number:
MFCD00132404
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

bovine

Quality Level

300

form

lyophilized powder

specific activity

≥3,000 units/mg protein

mol wt

32.5 kDa

composition

Protein, ≥95% biuret

storage condition

(Store under nitrogen.
Tightly closed. Dry.)

greener alternative product characteristics

Atom Economy
Design for Energy Efficiency
Use of Renewable Feedstocks
Learn more about the Principles of Green Chemistry.

technique(s)

immunoblotting: suitable
inhibition assay: suitable

color

blue-green

pI 

4.95

solubility

water: 20 mg/mL
aqueous buffer, pH 7.5: soluble

UniProt accession no.

P00442
P41976

application(s)

diagnostic assay manufacturing

greener alternative category

, Re-engineered

storage temp.

−20°C

Gene Information

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

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General description

Research area: Cell Signaling

Superoxide dismutase (SOD) is a redox-active metalloenzyme expressed in both aerobic and anaerobic living organisms. Bovine superoxide dismutase or CuZn SOD is a homodimer with each subunit containing one zinc and one copper ion.

Application

Superoxide dismutase from bovine erythrocytes has been used:

  • in a study to assess a kinetic model of radiation-induced inactivation of superoxide dismutase in nitrous oxide-saturated solutions
  • in a study to investigate the possible participation of superoxide anion in the intestinal tryptophan 2,3-dioxygenase reaction
  • to investigate its effect on the hemolysis rate of human RBCs and hemoglobin-nitric oxide complex (HbNO) stability in human erythrocytes
  • in combination with catalase to study its effect on cell differentiation in vitro
  • to quantify superoxide levels and study their effect on reactivity in mouse pulmonary arteries through chemiluminescence and cytochrome C reduction methods

Biochem/physiol Actions

Superoxide Dismutase from bovine erythrocytes catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. It serves as an antioxidant and 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.

Physical form

Lyophilized powder, essentially salt-free

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)

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Possible participation of superoxide anion in the intestinal tryptophan 2,3-dioxygenase reaction.
F Hirata et al.
The Journal of biological chemistry, 246(24), 7825-7826 (1971-12-25)
Sebastian Overmans et al.
Aquatic toxicology (Amsterdam, Netherlands), 198, 165-174 (2018-03-20)
Exposure to polycyclic aromatic carbons (PAHs) poses a growing risk to coral reefs due to increasing shipping and petroleum extraction in tropical waters. Damaging effects of specific PAHs can be further enhanced by the presence of ultraviolet radiation, known as
Colleen M Hansel et al.
mBio, 10(2) (2019-03-14)
There is a growing appreciation within animal and plant physiology that the reactive oxygen species (ROS) superoxide is not only detrimental but also essential for life. Yet, despite widespread production of extracellular superoxide by healthy bacteria and phytoplankton, this molecule
C A Chuaqui et al.
Biochimica et biophysica acta, 702(1), 112-116 (1982-03-18)
It has been reported that the inactivation yield of superoxide dismutase from bovine erythrocytes irradiated in N2O-saturated solutions increases exponentially with the initial enzyme concentration and that dose-response curves are non-exponential. The present work analyses these data using a kinetic
Tomohiro Furukawa et al.
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Aflatoxin contamination of crops is a worldwide problem, and elucidation of the regulatory mechanism of aflatoxin production, for example relative to the oxidative⁻antioxidative system, is needed. Studies have shown that oxidative stress induced by reactive oxygen species promotes aflatoxin production.
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Articles

Mitochondrial Stress and ROS

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

Enzymatic Assay of Superoxide Dismutase

HPLC Analysis of Superoxide Dismutase on Discovery® BIO PolyMA-WAX

Separation of Superoxide dismutase

Chromatograms

application for HPLC

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