Superoxide Dismutase

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More and more scientific evidence shows that reactive oxygen species (ROS) and reactive nitrogen species are important mediators of signaling events in cells, especially the superoxide anion in reactive oxygen species. If the content of superoxide anion in the human body is too high, it may induce various diseases, including pro-inflammatory diseases (pro-inflammatory diseases), cardiovascular diseases, neurological diseases (neurological diseases), diabetes, and radiation therapy, degeneration (fibrosis) and aging, etc.

To reduce the content of oxygen metabolites in tissues, thereby inhibiting inflammation, preventing the above-mentioned diseases, or preventing premature aging, it is necessary to appropriately supplement antioxidant enzymes. In addition to supplementing antioxidant enzymes from the outside world, in fact, most organisms have an important antioxidant enzyme called superoxide dismutase. This enzyme prevents cascade reactions of reactive oxygen species (ROS) and reactive nitrogen species (RNS).

As early as 1960, scientists discovered that superoxide dismutase has anti-inflammatory properties, so they are actively researching, hoping to find this substance from living organisms. After several studies and analysis, a protein called orgotein was finally isolated from beef liver. In 1968, American scholars McCord and Fridovich further research confirmed that this protein called orgotein has the enzymatic activity of removing superoxide anion, which helps to remove reactive oxygen species in the organism. Therefore, this kind of orgotein that can resist reactive oxygen species is called superoxide dismutase. Since then, the research and application of superoxide dismutase has received widespread attention from researchers of different professions and disciplines in the world.

In 1969, McCord and others further published an article in the American Journal of Biochemistry, expounding the biological significance of superoxide anion free radicals and superoxide dismutase (SOD), and pointing out their relationship with free radicals. Since then, it has broadened the horizons of researchers, significantly increased the interest of the biological and medical circles, and made breakthroughs in the study of free radicals. For example, the theory of aging and free radicals proposed by Professor Harman in 1956 has been verified, supplemented and developed.

In June 1976, the European Society of Molecular Biology held the first symposium on superoxide and superoxide dismutase in Banyuls, France. After the meeting, the discussion results were compiled and published. In the preface to the collection, Professor Michelson particularly praised the achievements of McCord and Friedovich. He believes that the two scientists first discovered the activity of superoxide dismutase from bovine red blood cells, and that superoxide free radicals have biological significance. This series of innovations laid a solid foundation for the subsequent research on molecular biology such as oxygen metabolism. Its achievements are almost comparable to the famous double helix theory of DNA published by Watson and Crick in 1953.

Superoxide dismutase is the first antioxidant enzyme that is most valued by researchers. Since its discovery more than 40 years ago, there have been more than 42,000 related research papers, and the number is increasing rapidly every year. The main reason is that superoxide dismutase has a variety of physiological functions, which can protect the organism from damage by reactive oxygen species (free radicals). Scientific evidence in recent years has shown that SOD actually helps maintain animal and human health. Therefore, it has been widely used in recent years, and it was first made into an industrial enzyme. It has been used as a pharmaceutical since 1990, mainly used to improve the inflammatory response caused by the disease, and the sequelae or side effects caused by it, such as tissue fibrosis caused by cancer patients receiving radiation therapy.

More information can be found at https://www.creative-enzymes.com/similar/sod_659.html.

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