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S8160

Sigma-Aldrich

Superoxide Dismutase from bovine liver

lyophilized powder, ≥1500 units/mg protein

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.54

form

lyophilized powder

Quality Level

specific activity

≥1500 units/mg protein

mol wt

32.5 kDa

composition

Protein, ≥70% biuret

UniProt accession no.

storage temp.

−20°C

Gene Information

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General description

Research area: Cell signalingSuperoxide Dismutase (SOD), a low molecular weight protein that is found in all aerobic cells of microorganisms, plants, and animals. It exists as three distinct families such as manganese SOD, copper–zinc SOD, and extracellular SOD.

Application

Superoxide dismutase from bovine liver has been used in a study to determine that hypercholesterolemia increases endothelial superoxide anion production. Superoxide dismutase from bovine liver has also been used in a study to investigate diazo coupling, subunit interactions, and electrophoretic variants of bovine erythrocyte superoxide dismutase. It has also been used as a component of the assay buffer in thequantification of reactive oxygen species (ROS) by O2k fluorometry.

Biochem/physiol Actions

Superoxide Dismutase catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. It plays a critical role in the defense of cells against the toxic effects of oxygen radicals. It 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 containing potassium phosphate buffer salts

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

10 - Combustible liquids

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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Characterisation by EPR spectroscopy of the co-ordination environment of copper in superoxide dismutase from horseradish (Armoracia rusticana Gaertn.)
Palivan, CG and Palivan, H
Proceedings of the Royal Society of Edinburgh. Section B: Biology, 102, 273-277 (1994)
Bovine erythrocyte superoxide dismutase: diazo coupling, subunit interactions, and electrophoretic variants.
D P Malinowski et al.
Biochemistry, 18(1), 237-244 (1979-01-09)
S D Yan et al.
The Journal of biological chemistry, 269(13), 9889-9897 (1994-04-01)
Attack by reactive oxygen intermediates, common to many kinds of cell/tissue injury, has been implicated in the development of diabetic and other vascular diseases. Such oxygen-free radicals can be generated by advanced glycation end products (AGEs), which are nonenzymatically glycated
Y Ohara et al.
The Journal of clinical investigation, 91(6), 2546-2551 (1993-06-01)
Indirect evidence suggests accelerated degradation of endothelium-derived nitric oxide (ENDO) by superoxide anion (O2-) in hypercholesterolemic vessels (HV). To directly measure O2- production by normal vessels (NV) and HV, we used an assay for O2- based on the chemiluminescence (CL)
Naoya Ichimaru et al.
Biochemistry, 47(40), 10816-10826 (2008-09-11)
The mode of action of Deltalac-acetogenins, strong inhibitors of bovine heart mitochondrial complex I, is different from that of traditional inhibitors such as rotenone and piericidin A [Murai, M., et al. (2007) Biochemistry 46 , 6409-6416]. As further exploration of

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