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S5395

Sigma-Aldrich

Superoxide Dismutase from bovine erythrocytes

BioReagent, ≥3,000 units/mg protein, lyophilized powder, suitable for cell culture

Synonym(s):

SOD, Superoxide: superoxide oxidoreductase

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.75

biological source

bovine erythrocytes

product line

BioReagent

form

lyophilized powder

specific activity

≥3,000 units/mg protein

mol wt

32.5 kDa

packaging

pkg of 15000 units

technique(s)

cell culture | mammalian: suitable

pH

7.6-10.5

shipped in

dry ice

storage temp.

−20°C

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General description

Superoxide Dismutase from bovine erythrocytes is a metalloprotein which disproportionates superoxide anion radicals. It is a 31.5 kDa copper binding protein and displays a conserved domain and fold. It is a homodimer with one copper and zinc ion per subunit and has antiparallel “greek-key” β barrel fold.

Application

Superoxide Dismutase (SOD) from bovine erythrocytes has been used:
  • for measuring the superoxide radical using the electron paramagnetic resonance spin in human brain microvascular endothelial cells
  • for measuring superoxide production in cytochrome C assay in peripheral blood mononuclear cells
  • as a standard in characterization of hen egg SOD using Fourier-transform infrared spectroscopy (FTIR) and matrix-assisted laser desorption/ionization (MALDI) analysis

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.

Analysis Note

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

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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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The structural biochemistry of the superoxide dismutases
Perry JJP, et al.
Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics, 1804(2), 245-262 (2010)
Partial biochemical characterization of Cu, Zn-superoxide dismutase extracted from eggs of hens (Gallus gallus domesticus)
Wawrzykowski J and Kankofer M
Food Chemistry, 227, 390-396 (2017)
Structure of fully reduced bovine copper zinc superoxide dismutase at 1.15
Hough MA and Hasnain SS
Structure, 11(8), 937-946 (2003)
Felix Christen et al.
Conservation physiology, 8(1), coaa108-coaa108 (2021-01-08)
The cardiovascular system is a major limiting system in thermal adaptation, but the exact physiological mechanisms underlying responses to thermal stress are still not completely understood. Recent studies have uncovered the possible role of reactive oxygen species production rates of
Zoe Loomis et al.
PloS one, 12(2), e0171219-e0171219 (2017-02-06)
It is now well established that both inherited and acquired forms of hemolytic disease can promote pulmonary vascular disease consequent of free hemoglobin (Hb) induced NO scavenging, elevations in reactive oxygen species and lipid peroxidation. It has recently been reported

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