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S8409

Sigma-Aldrich

Superoxide Dismutase from bovine liver

ammonium sulfate suspension, 2,000-6,000 units/mg protein (biuret)

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

form

ammonium sulfate suspension

Quality Level

specific activity

2,000-6,000 units/mg protein (biuret)

mol wt

32.5 kDa

UniProt accession no.

storage temp.

2-8°C

Gene Information

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S7446S8160S9697
vibrant-m

S9697

Superoxide Dismutase bovine

specific activity

2,000-6,000 units/mg protein (biuret)

specific activity

≥4,500 units/mg protein

specific activity

≥1500 units/mg protein

specific activity

≥2500 units/mg protein

form

ammonium sulfate suspension

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

mol wt

32.5 kDa

mol wt

32.5 kDa

mol wt

32.5 kDa

mol wt

-

UniProt accession no.

P00442

UniProt accession no.

-

UniProt accession no.

P00442

UniProt accession no.

A4URH1

General description

Superoxide dismutases are a group of low molecular weight metalloproteins present in all aerobic cells of plants, animals and micro-organisms. They provide protection against damaging reactions with the superoxide radical anion (O2-) by catalyzing its disproportionation into oxygen and hydrogen peroxide.

Application

Superoxide Dismutase from bovine liver has been used:
  • for measuring mitochondrial hydrogen peroxide production in skeletal muscle
  • as a positive control in Cu(II) binding stability assay
  • as a positive control in superoxide dismutase assay

Superoxide dismutase from bovine liver has been used in a study to assess the inactivation of endothelial derived relaxing factor by oxidized lipoproteins. Superoxide dismutase from bovine liver has also been used in a study to investigate the role of hydrogen peroxide in the cytotoxicity of the xanthine/xanthine oxidase system.

Biochem/physiol Actions

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.

Physical form

Suspension in 3.8 M (NH4)2SO4, pH 7.0

Analysis Note

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

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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Perturbed redox signaling exacerbates a mitochondrial myopathy
Dogan SA, et al.
Cell Metabolism, 28(5), 764-775 (2018)
Exploiting the vulnerable active site of a copper-only superoxide dismutase to disrupt fungal pathogenesis
Robinett NG, et al.
The Journal of Biological Chemistry, jbc-RA118 (2018)
E M Link et al.
The Biochemical journal, 249(2), 391-399 (1988-01-15)
1. The survival of mammalian epithelial cells exposed in vitro to the xanthine/xanthine oxidase system in phosphate-buffered saline (PBS) or serum-containing medium (SCMEM) was investigated. 2. The cytotoxic effect observed depended on the composition of the medium in which the
L G Chi et al.
Circulation research, 64(4), 665-675 (1989-04-01)
Available data demonstrate that oxygen free radicals and derived reactive species of oxygen are produced during myocardial ischemia as well as upon reperfusion of the ischemic tissue. The present study was designed to determine if polyethylene glycol-conjugated superoxide dismutase (PEG-SOD)
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

Articles

Instructions for working with enzymes supplied as ammonium sulfate suspensions

Protocols

Enzymatic Assay of Superoxide Dismutase

Chromatograms

application for HPLC

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