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脑细胞质骨架和膜组分中一种酸性钙调蛋白结合蛋白的特性分析。

The characterization of an acidic calmodulin-binding protein in brain cytoskeleton and membrane fractions.

作者信息

Strocchi P, Gilbert J M

出版信息

Biochem J. 1986 Dec 1;240(2):593-6. doi: 10.1042/bj2400593.

Abstract

One of the most abundant acidic proteins in rat brain has an Mr of 68,000 and a pI of 5.6 (68K 5.6 protein) when analysed by two-dimensional gel electrophoresis. The 68K 5.6 protein was found in large relative amounts in brain cytoskeleton preparations and in membrane and supernatant fractions. High-salt washing and proteolytic digestion did not remove this protein from the membrane elements. The 68K 5.6 protein was also found in the microtubule-associated protein fraction of purified microtubules and was present in large relative amounts in preparations of intermediate-filament proteins. The 68K 5.6 protein binds to calmodulin in the presence of Ca2+ ions, and we found it to be an abundant acidic calmodulin-binding protein in brain tissue.

摘要

大鼠脑中含量最为丰富的酸性蛋白之一,经二维凝胶电泳分析,其分子量为68,000,等电点为5.6(68K 5.6蛋白)。在脑细胞骨架制剂以及膜和上清液组分中发现,68K 5.6蛋白的相对含量较高。高盐洗涤和蛋白水解消化均未能从膜成分中去除该蛋白。在纯化微管的微管相关蛋白组分中也发现了68K 5.6蛋白,并且在中间丝蛋白制剂中的相对含量也较高。68K 5.6蛋白在Ca2+离子存在的情况下与钙调蛋白结合,我们发现它是脑组织中一种丰富的酸性钙调蛋白结合蛋白。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6a52/1147454/445b10a7bb0c/biochemj00266-0270-a.jpg

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