PHOSPHORYLATION OF CHICK LENS PROTEINS
PHOSPHORYLATION OF CHICK LENS PROTEINS
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DOI：
10.3109/02713688409167214
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发表时间：
1984-01-01
影响因子：
2
通讯作者：
MAISEL, H
中科院分区：
文献类型：
--
作者：
IRELAND, M;MAISEL, H
鸡透镜的磷酸化蛋白质在含有32 P的培养基中孵育后鉴定，随后通过凝胶电泳进行分析。波形蛋白的酸性变体和胞衬蛋白的两个亚基被磷酸化，与珠状链丝相关的95 Kd [千道尔顿]和49 Kd蛋白也被磷酸化。晶体蛋白和主要的内在膜蛋白都没有磷酸化。上皮细胞的几种低分子量磷蛋白在纤维细胞中不存在。
Phosphorylated proteins of the chick lens were identified following incubation of lenses in a medium containing 32P and subsequent analysis by gel electrophoresis. The acidic variant of vimentin and both subunits of fodrin were phosphorylated, as were the 95 Kd [kilodaltons] and 49 Kd proteins associated with the beaded-chain filaments. Neither crystallins nor the main intrinsic membrane proteins were phosphorylated. Several low MW phosphoproteins of the epithelial cell were not present in the fiber cells.