S8160
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:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-943-0
MDL number:
Product Name
Superoxide Dismutase from bovine liver, lyophilized powder, ≥1500 units/mg protein
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
Quality Level
Gene Information
cow ... SOD1(281495)
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Analysis Note
For assay method, see McCord, J.M. and Fridovich, I., J. Biol. Chem., 244, 6049 (1969).
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.
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.
Other Notes
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
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
低风险生物材料
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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)
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
Protocols
Enzymatic Assay of Superoxide Dismutase
Separation of Superoxide dismutase
在测定超氧化物歧化酶活性时，使用了一种在550 nm处的连续分光光度法进行测定。一个酶单位可将酶偶联系统的细胞色素c还原率抑制50％。
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