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鸡晶状体蛋白的磷酸化作用。

Phosphorylation of chick lens proteins.

作者信息

Ireland M, Maisel H

出版信息

Curr Eye Res. 1984 Jul;3(7):961-8. doi: 10.3109/02713688409167214.

DOI:10.3109/02713688409167214
PMID:6467970
Abstract

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 the vimentin and both subunits of fodrin were phosphorylated, as were the 95 Kd and 49 Kd proteins associated with the beaded-chain filaments. Neither crystallins nor the main intrinsic membrane proteins were phosphorylated. Several low molecular weight phosphoproteins of the epithelial cell were not present in the fiber cells.

摘要

在含有³²P的培养基中孵育鸡晶状体,随后通过凝胶电泳进行分析,鉴定出了鸡晶状体中的磷酸化蛋白。波形蛋白的酸性变体和血影蛋白的两个亚基都发生了磷酸化,与串珠状细丝相关的95 Kd和49 Kd蛋白也发生了磷酸化。晶状体蛋白和主要内在膜蛋白均未发生磷酸化。上皮细胞的几种低分子量磷蛋白在纤维细胞中不存在。

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A novel terminal web-like structure in cortical lens fibers: architecture and functional assessment.皮质晶状体纤维中存在一种新颖的终末网状结构:结构与功能评估。
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Posttranslational modifications of the bovine lens beaded filament proteins filensin and CP49.
牛晶状体串珠丝蛋白 filensin 和 CP49 的翻译后修饰。
Invest Ophthalmol Vis Sci. 2010 Mar;51(3):1565-74. doi: 10.1167/iovs.09-4565. Epub 2009 Oct 29.
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Lens intermediate filaments.晶状体中间丝。
Exp Eye Res. 2009 Feb;88(2):165-72. doi: 10.1016/j.exer.2008.11.007. Epub 2008 Nov 24.
5
Filensin and phakinin form a novel type of beaded intermediate filaments and coassemble de novo in cultured cells.丝状晶蛋白和晶丝蛋白形成一种新型的串珠状中间丝,并在培养细胞中重新组装。
J Cell Biol. 1996 Feb;132(4):643-55. doi: 10.1083/jcb.132.4.643.
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Bovine filensin possesses primary and secondary structure similarity to intermediate filament proteins.牛丝状肌动蛋白与中间丝蛋白在一级和二级结构上具有相似性。
J Cell Biol. 1993 May;121(4):847-53. doi: 10.1083/jcb.121.4.847.
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cAMP-dependent phosphorylation of bovine lens alpha-crystallin.牛晶状体α-晶状体蛋白的环磷酸腺苷(cAMP)依赖性磷酸化
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