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钙调蛋白调节的真核生物延伸因子2激酶与热休克蛋白90的相互作用。

Interaction of the calcium and calmodulin regulated eEF-2 kinase with heat shock protein 90.

作者信息

Palmquist K, Riis B, Nilsson A, Nygård O

机构信息

Department of Zoological Cell Biology, Arrhenius Laboratories E5, Stockholm University, Sweden.

出版信息

FEBS Lett. 1994 Aug 1;349(2):239-42. doi: 10.1016/0014-5793(94)00676-8.

Abstract

Immunoadsorbents containing the 8D3 anti-heat shock protein 90 monoclonal antibodies were prepared. Partly purified preparations of the Ca2+ and calmodulin dependent eukaryotic elongation factor eEF-2 specific kinase and crude rabbit reticulocyte lysates were mixed with the immunoadsorbent. After removal of unbound proteins the adsorbed material was released by increasing the salt concentration in the buffer. Analysis of the bound material showed that the eEF-2 kinase was bound to the immunoadsorbent together with hsp 90. The adsorption of the kinase was found to depend on the presence of hsp 90.

摘要

制备了含有8D3抗热休克蛋白90单克隆抗体的免疫吸附剂。将部分纯化的Ca2+和钙调蛋白依赖性真核延伸因子eEF-2特异性激酶制剂与粗制兔网织红细胞裂解物与免疫吸附剂混合。去除未结合的蛋白质后,通过增加缓冲液中的盐浓度释放吸附的物质。对结合物质的分析表明,eEF-2激酶与hsp 90一起结合到免疫吸附剂上。发现激酶的吸附取决于hsp 90的存在。

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