SPECIFICITY OF ALPHA-CRYSTALLIN BINDING TO THE LENS MEMBRANE
SPECIFICITY OF ALPHA-CRYSTALLIN BINDING TO THE LENS MEMBRANE
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DOI：
10.3109/02713689009044521
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发表时间：
1990-03-01
影响因子：
2
通讯作者：
TAKEMOTO, L
中科院分区：
文献类型：
--
作者：
IFEANYI, F;TAKEMOTO, L
牛α晶状体蛋白的A1、A2、B1和B2种类已被纯化和复性以形成仅由一种种类组成的高分子量聚集体，并且这些种类中的每一种的聚集形式已被测试它们在体外结合到透镜膜的能力。α-A1和α-A2的聚集形式以可饱和的方式结合到膜上，而α-B1和α-B2的聚集形式以与可饱和结合不一致的方式以低得多的量结合。总之，这些结果证明了聚集的α-A1和α-A2与透镜膜的特异性和可饱和结合，表明这些物质负责先前观察到的α晶体蛋白和透镜纤维细胞膜之间的相互作用。
The A1, A2, B1, and B2 species of bovine alpha crystallin have been purified and renatured to form high molecular weight aggregates comprised of only one species, and the aggregated forms of each of these species have been tested for their ability to bind to lens membrane in vitro. The aggregated forms of alpha-A1 and alpha-A2 bound to membrane in a saturable manner while those of alpha-B1 and alpha-B2 bound in much lower amounts, in a manner inconsistent with saturable binding. Together, these results demonstrate specific and saturable binding of aggregated alpha-A1 and alpha-A2 to the lens membrane, suggesting that these species are responsible for the previously observed interaction between alpha crystallin and the lens fiber cell membrane.