Yan Langzi, a researcher at the National Center for Psychiatry and Neurology of Japan, recently discovered two substances that can suppress the abnormality of Prion prion protein and may help to develop drugs for preventing mad cow disease. Prion prion protein abnormalities are responsible for mad cow disease and Jacob's disease in humans, but the pathogenesis of prion protein abnormalities in humans has not yet been clarified. The substance that prevents BSE from mad cow disease discovered by Naoko Iwana is copper chlorophyllin and iron sodium chlorophyllin, which are similar to chlorophyll, and are commonly used in food additives and pharmaceuticals, and have a high food safety. It is generally believed that the normal Prion protein is mutated after the variant Prion protein is attached. Proliferation of the variant protein leads to mad cow disease and Jacob's disease in humans. When Iwawako looks for substances that block the attachment of abnormal stereostructure prions to normal sialoproteins, he found through cell experiments that sodium copper chlorophyllate and sodium iron chlorophyllin could prevent normal Prion protein variation. Naoko Iwana first used gene technology to develop mouse neural cells that can both synthesize normal prion protein and generate variants of the protein, and then added copper copper chlorophyllin and iron sodium chlorophyllin to nerve cells. As a result of the aqueous solution, it was found that normal prion protein was not mutated, and it was proved that sodium copper chlorophyllate and iron sodium chlorophyllite inhibit the production of abnormal prion protein. Normal Prion protein includes a helical structure and a ribbon structure. Yan Langzi believes that in the three-dimensional structure of normal prion protein, when the mutant Prion protein attaches to the normal Prion prion protein band structure, the band structure will become a spiral, resulting in normal prion mutation. Sodium copper chlorophyllin and sodium iron chlorophyllate adhere to the normal Plion band structure before the mutant Prion, thereby preventing structural changes in the Pr protein.
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