The influence of some post-translational modifications on the chaperone-like activity of alpha-crystallin.
The influence of some post-translational modifications on the chaperone-like activity of alpha-crystallin.
复制标题
一些翻译后修饰对α-晶状体蛋白的分子伴侣样活性的影响。
DOI：
10.1159/000267940
复制
发表时间：
1996
影响因子：
2.1
通讯作者：
W. D. de Jong
中科院分区：
文献类型：
--
作者：
M. V. van Boekel;S. Hoogakker;J. Harding;W. D. de Jong
We investigated the influence of phosphorylation, glycation, carbamylation and oxidative modification on the capacity of alpha-crystallin to protect beta-crystallins against heat denaturation. Simple modification of lysine residues by early glycation or carbamylation had no effect. However, late (cross-linking) glycation products and oxidative modifications decreased the chaperone-like activity of alpha-crystallin. Homopolymers of alpha A-crystallin had a higher protecting capacity compared with those of alpha B-crystallin. The in vivo phosphorylated forms of especially alpha A- but also alpha B-crystallin revealed a somewhat better protecting ability than the respective non-phosphorylated forms.
