Garland D, Zigler J S, Kinoshita J
Arch Biochem Biophys. 1986 Dec;251(2):771-6. doi: 10.1016/0003-9861(86)90389-9.
Ascorbate, Fe3+, or Cu2+ and oxygen induced the oxidation of bovine lens crystallins. The modifications mimicked those that occur in the lens with aging. The modifications included the formation of nondisulfide crosslinks in alpha- and beta H-crystallin and the cleavage of alpha-, beta H-, and the low molecular weight crystallin fractions. In all three fractions, there was a loss of the more basic protein species and an increase in the more acidic species. Nontryptophan fluorescence with emission spectra between 400 and 500 nm was produced in beta H-crystallin. Cu2+ was less effective than Fe3+ in catalyzing the modification of beta H- and gamma-crystallin. Both metal ions were equally effective in catalyzing the modification of alpha-crystallin.
抗坏血酸盐、Fe3+、Cu2+和氧气会诱导牛晶状体晶状体蛋白发生氧化。这些修饰模拟了晶状体随年龄增长而出现的变化。修饰包括在α-和β-H晶状体蛋白中形成非二硫键交联以及α-、β-H-和低分子量晶状体蛋白组分的裂解。在所有这三个组分中，碱性更强的蛋白质种类减少，酸性更强的种类增加。β-H晶状体蛋白产生了发射光谱在400至500纳米之间的非色氨酸荧光。在催化β-H-和γ-晶状体蛋白的修饰方面，Cu2+的效果不如Fe3+。两种金属离子在催化α-晶状体蛋白的修饰方面效果相当。
