Covalent change in alpha crystallin during human senile cataractogenesis.
Covalent change in alpha crystallin during human senile cataractogenesis.
复制标题
人类老年性白内障发生过程中α晶状体蛋白的共价变化。
DOI：
10.1016/0006-291x(88)90726-7
复制
发表时间：
1988
影响因子：
3.1
通讯作者：
R. Wong
中科院分区：
文献类型：
--
作者：
L. Takemoto;D. Granstrom;T. Kodama;R. Wong
用sds -聚丙烯酰胺凝胶电泳技术对正常人和白内障晶状体核的高分子量聚集体（HMWA）进行了分离，并用针对整个α -晶体蛋白分子的抗血清和针对α -晶体蛋白合成肽（α - A2 147 - 161和α - A2 163-173）的抗血清对α -晶体蛋白带进行了探测。这些抗血清结合的定量结果表明，抗alphaa2 163 - 173血清和抗alphawholesera与来自正常和白内障晶状体的HMWA片段的α结晶蛋白带结合同样良好。相比之下，抗α a2 147 - 161血清与来自正常晶状体的α结晶蛋白结合很少，如果有的话，而与来自白内障晶状体的α结晶蛋白结合良好。这些结果证明了α晶体蛋白分子的共价改变，并提出了在老年人类晶状体白内障形成过程中可能发生的共价变化的可能位置。
The high molecular weight aggregates (HMWA) obtained from normal and cataractous human lens nuclei have been resolved by SDS-polyacrylamide gel electrophoresis, and the alpha crystallin band has been probed with antisera made against the whole alpha crystallin molecule and with antisera made against synthetic peptides of alpha crystallin (alphaA2 147–161and alpha A2 163–173). Quantitation of these antisera binding demonstrated that the anti-alphaA2 163–173serum and the anti-alphawholesera bound equally well to the alpha crystallin band from the HMWA fraction from normal and cataractous lenses. In contrast, the anti-alphaA2 147–161serum bound little, if at all, to alpha crystallin from normal lenses, while it bound well to alpha crystallin from cataractous lenses. These results demonstrate a covalent alteration in the alpha crystallin molecule, and suggest a possible location of a covalent change that may occur during the cataractogenic process in the aged human lens.