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连接蛋白的一种新结构域序列定位于骨骼肌肌节的I带:与神经丝亚基的同源性。

A novel domain sequence of connectin localized at the I band of skeletal muscle sarcomeres: homology to neurofilament subunits.

作者信息

Maruyama K, Endo T, Kume H, Kawamura Y, Kanzawa N, Nakauchi Y, Kimura S, Kawashima S, Maruyama K

机构信息

Department of Molecular Biology, Tokyo Metropolitan Institute of Medical Science, Japan.

出版信息

Biochem Biophys Res Commun. 1993 Aug 16;194(3):1288-91. doi: 10.1006/bbrc.1993.1963.

Abstract

A cDNA of 4.0 kb was cloned from a chicken embryo skeletal muscle cDNA library, using an antibody to muscle elastic protein connectin (titin), the molecular mass of which is estimated to be 3,000 kDa. Immunoelectron microscopy revealed that the antiserum raised against the product of the cDNA expressed in E. coli bound to the epitopes of the connectin filament near the N2 line of chicken breast muscle sarcomeres. The predicted amino acid sequence contains eight immunoglobulin C2 motifs and regions highly homologous with the high and medium molecular weight subunits of neurofilament. In addition, there are regions homologous with desmoplakin, calsequestrin, and calpastatin.

摘要

利用针对肌肉弹性蛋白连接蛋白(肌联蛋白)的抗体,从鸡胚骨骼肌cDNA文库中克隆出一个4.0 kb的cDNA,其分子量估计为3000 kDa。免疫电子显微镜显示,针对在大肠杆菌中表达的cDNA产物产生的抗血清与鸡胸肌肌节N2线附近的连接蛋白丝的表位结合。预测的氨基酸序列包含八个免疫球蛋白C2基序以及与神经丝高分子量和中分子量亚基高度同源的区域。此外,还有与桥粒斑蛋白、肌钙蛋白和钙蛋白酶抑制蛋白同源的区域。

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