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目的：观察维生素Ｃ（ＡＳＡ）在晶体蛋白发生光氧化时的作用及其机制。方法：牛晶体蛋白溶液在加入或不加入ＡＳＡ时，于５天内共接受２００ｍＪ／ｃｍ２紫外线Ｂ（ＵＶＢ）照射，接着在３７℃继续孵育至第３周，然后测定晶体蛋白的非色氨酸荧光、游离巯基和进行蛋白电泳分析。结果：ＡＳＡ在溶液中易被氧化，蛋白溶液中加入ＡＳＡ促使晶体蛋白的非色氨酸荧光产生明显增强，导致非二硫键聚合形成，对晶体蛋白的游离巯基减少有保护作用。有ＡＳＡ时，ＵＶＢ照射更易导致晶体蛋白形成非二硫键聚合。结论：体外溶液中的ＡＳＡ易与晶体蛋白发生糖化作用，同时作为抗氧化剂能保护晶体蛋白的游离巯基不被氧化。
Objective: To observe the effect of vitamin C (ASA) on the photoprotection of crystal protein and its mechanism. METHODS: Bovine lens protein solution was exposed to UVB (UVB) at 200 mJ / cm2 for 5 days with and without addition of ASA, followed by incubation at 37 ° C until the third week. The non-tryptophan fluorescence of the crystal protein , Free thiol and protein electrophoretic analysis. RESULTS: ASA was easily oxidized in solution. ASA was added to the protein solution to enhance the non-tryptophan fluorescence of crystal protein, resulting in the polymerization of non-disulfide bonds and the decrease of free thiol of crystal protein. In the presence of ASA, UVB irradiation more easily led to the formation of non-disulfide polymerization of crystal proteins. CONCLUSION: ASA in vitro solution is easy to mash with crystalline protein, and at the same time it acts as an anti-oxidant to protect the free sulfhydryl of crystal protein from being oxidized.