| Powder: | Yes |
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| Customized: | Customized |
| Certification: | ISO 9001, USP |
| Suitable for: | Elderly, Adult |
| State: | Solid |
| Purity: | >99% |
| Samples: |
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| Customization: |
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Product Name: superoxide dismutase
Cas No.: 9054-89-1
EINECS: 232-943-0
Appearance: White or light blue crystalline powder
Enzyme activity: 1000U/mg-6000U/mg
PH: 6.5~7.6
Protein content: 85%
Description
SOD Enzyme is an enzyme that alternately catalyzes the dismutation (or partitioning) of the superoxide (O2−) radical into either ordinary molecular oxygen (O2) or hydrogen peroxide(H2O2). Superoxide is produced as a by-product of oxygen metabolism and, if not regulated, causes many types of cell damage. Hydrogen peroxide is also damaging, but less so, and is degraded by other enzymes such as catalase. Thus, SOD is an important antioxidant defense in nearly all living cells exposed to oxygen. One exception is Lactobacillus plantarum and related lactobacilli, which use a different mechanism to prevent damage from reactive (O2−).
SOD enzymes deal with the superoxide radical by alternately adding or removing an electron from the superoxide molecules it encounters, thus changing the O2− into one of two less damaging species: either molecular oxygen (O2) or hydrogen peroxide (H2O2). This SOD-catalyzed dismutation of superoxide may be written, for Cu,Zn SOD, with the following half-reactions:
Cu2+-SOD + O2− → Cu+-SOD + O2
Cu+-SOD + O2− + 2H+ → Cu2+-SOD + H2O2
The general form, applicable to all the different metal-coordinated forms of SOD, can be written as follows:
M(n+1)+-SOD + O2− → Mn+-SOD + O2
Mn+-SOD + O2− + 2H+ → M(n+1)+-SOD + H2O2.
where M = Cu (n=1) ; Mn (n=2) ; Fe (n=2) ; Ni (n=2).
In a series of such reactions, the oxidation state and the charge of the metal cation oscillates between n and n+1: +1 and +2 for Cu, or +2 and +3 for the other metals.
Several common forms of SOD exist: they are proteins whose active site uses copper and zinc, or manganese, iron, or nickel. Thus, there are three major families of superoxide dismutase, depending on the protein fold and the metal cofactor:
the Cu/Zn type (which binds both copper and zinc);
Fe and Mn types (which bind either iron or manganese);
Ni type, which binds nickel.
Application
Activity
SOD has powerful antinflammatory activity. For example, SOD is a highly effective experimental treatment of chronic inflammation in colitis. Treatment with SOD decreases reactive oxygen species generation and oxidative stress and, thus, inhibits endothelial activation and indicate that modulation of factors that govern adhesion molecule expression and leukocyte-endothelial interactions. Therefore, such antioxidants may be important new therapies for the treatment of inflammatory bowel disease.
Cosmetic uses
SOD may reduce free radical damage to skin-for example, to reduce fibrosis following radiation for breast cancer. Studies of this kind must be regarded as tentative, however, as there were not adequate controls in the study including a lack of randomization, double-blinding, or placebo. Superoxide dismutase is known to reverse fibrosis, perhaps through reversion of myofibroblasts back to fibroblasts.
Commercial sources
SOD is commercially obtained from bovine liver, horseradish, cantaloupe and by fermenting certain bacteria, though it is found in most living forms at diverse concentrations. For therapeutic purpose, SOD is usually injected locally. There is no evidence that ingestion of unprotected SOD or SOD-rich foods can have any physiological effects: as all ingested SOD is broken down into amino acids before being absorbed. However, ingestion of SOD bound to wheat proteins could improve its therapeutic activity, at least in theory.
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