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Merck

S8160

Sigma-Aldrich

Superoxide Dismutase from bovine liver

lyophilized powder, ≥1500 units/mg protein

Sinónimos:

SOD, Superoxide: superoxide oxidoreductase

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About This Item

Número de CAS:
Comisión internacional de enzimas:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

form

lyophilized powder

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

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Bovine erythrocyte superoxide dismutase: diazo coupling, subunit interactions, and electrophoretic variants.
D P Malinowski et al.
Biochemistry, 18(1), 237-244 (1979-01-09)
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)
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)
Lu Miao et al.
Free radical biology & medicine, 47(4), 344-356 (2009-05-30)
Numerous short-lived and highly reactive oxygen species (ROS) such as superoxide (O2(.-)), hydroxyl radical, and hydrogen peroxide are continuously generated in vivo. Depending upon concentration, location, and intracellular conditions, ROS can cause toxicity or act as signaling molecules. The cellular
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

Protocolos

Enzymatic Assay of Superoxide Dismutase

Chromatograms

application for HPLC

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