| Glutathione peroxidase (GPX) is one of the most important antioxidantenzymes in organisms, which distributes extensively in cell, blood, and tissues.GPXs prevent the organism from the damage of free radicals by scavenginghydrogen peroxide and lipid hydroperoxide, and maintain the normallyphysiological functions of the cells and tissues. Modern medicine studies onreactive oxygen species (ROS), including superoxide anion, hydroperoxides,hydroxyl radical, and single oxygen, showed that the metabolic disorder of freeradocals is believed to cause many diseases, such as cataract, diabetes, Keshandisease and some cardiovascular disease. Thus it has very important perspective indrug development. For the disadvantages of native GPX, such as instability andlimited availability, it is hard to be prepared extensively. Since 1980's, the artificialmimic of GPX has provided a new method for the drug development of GPX. Theearly mimics of GPX were small seleno-containing organic chemicals, whose GPXactivities were rather low compared to native GPX and the toxicity of them is large.Our group has successively synthesized a series of GPX mimics includingseleno-cyclodextrins and selenium containing catalytic antibodies since the end of1980's.Recently, our group successively expressed scFv 2F3 that contains GSHbinding site using protein engineering method, converted it to be selenium-containing scFv by chemical mutation and implemented the expression ofsingle-chain antibody as a soluble protein by constructing the new expressionstrain. On the basis of previous work, we carried out the researches for protectingeffect of selenium containing single-chain antibody Se-scFv2F3 to cardiac musclecells and liver cells from oxidation damage.In Chapter 1, we introduced the character of GPX, the artificial mimic ofGPX and the cloning, expression and purification of selenium containingsingle-chain antibody. In Chapter 2,the protection of cardiac muscle cells from...
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