Isolation of alpha-crystallin subunits by gel filtration.
Isolation of alpha-crystallin subunits by gel filtration.
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通过凝胶过滤分离α-晶状体蛋白亚基。
DOI：
10.3109/02713688709034839
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发表时间：
1987
影响因子：
2
通讯作者：
R. Augusteyn
中科院分区：
文献类型：
--
作者：
A. Stevens;R. Augusteyn
在pH 2.5的0.1M甘氨酸存在下，α-晶体蛋白解离成只含有αA链和单体αB链的聚集体。利用这一点，开发了一种通过Sephadex G-75凝胶过滤纯化αA和αB链的方法。这种方法提供了高产率的纯化亚基，并避免了与其他使用高浓度尿素的方法相关的氨甲酰化风险。
In the presence of 0.1 M glycine, pH 2.5, alpha-crystallin dissociates into aggregates containing only alpha A chains plus monomeric alpha B chains. Advantage has been taken of this to develop a method for the purification of the alpha A and alpha B chains by gel filtration on Sephadex G-75. This method gives high yields of purified subunits and avoids the risk of carbamylation associated with other methods which use high concentrations of urea.