Takemoto L, Granstrom D, Kodama T, Wong R
Division of Biology, Kansas State University, Manhattan 66506.
Biochem Biophys Res Commun. 1988 Feb 15;150(3):987-95. doi: 10.1016/0006-291x(88)90726-7.
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 (alpha A2 147-161 and alpha A2 163-173). Quantitation of these antisera binding demonstrated that the anti-alpha A2 163-173 serum and the anti-alpha whole sera bound equally well to the alpha crystallin band from the HMWA fraction from normal and cataractous lenses. In contrast, the anti-alpha A2 147-161 serum 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.
通过SDS-聚丙烯酰胺凝胶电泳解析了从正常和白内障人晶状体核中获得的高分子量聚集体（HMWA），并用针对整个α-晶体蛋白分子制备的抗血清以及针对α-晶体蛋白合成肽（αA2 147-161和αA2 163-173）制备的抗血清对α-晶体蛋白条带进行了检测。这些抗血清结合的定量分析表明，抗αA2 163-173血清和抗α全血清与正常和白内障晶状体HMWA组分中的α-晶体蛋白条带结合效果相同。相比之下，抗αA2 147-161血清与正常晶状体中的α-晶体蛋白几乎不结合（如果有结合的话），而与白内障晶状体中的α-晶体蛋白结合良好。这些结果证明了α-晶体蛋白分子中的共价改变，并提示了在老年人类晶状体白内障形成过程中可能发生共价变化的一个位置。
