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新生大鼠大脑中β蛋白前体的鉴定。

Identification of beta protein precursor in newborn rat brain.

作者信息

Takio K, Hasegawa M, Titani K, Ihara Y

机构信息

Frontier Research Program, RIKEN, Saitama, Japan.

出版信息

Biochem Biophys Res Commun. 1989 May 15;160(3):1296-301. doi: 10.1016/s0006-291x(89)80144-5.

Abstract

We have identified by protein sequencing the precursor of beta protein in newborn rat brain. A rabbit antibody was raised against a synthetic peptide corresponding to the carboxyl-terminal 30 residues (666-695) of the putative beta-amyloid protein precursor (Kang et al. 1987). The antiserum recognized multiple bands at 110-130 kD in the blot of Triton X-100 extract of newborn rat brain homogenates. The partially purified immunoreactive proteins were subjected to SDS-PAGE, electrophoretically transferred onto a polyvinylidene difluoride membrane and analyzed for the partial amino-terminal sequence. Each of the three major immunoreactive polypeptides yielded the same amino-terminal sequence of LEVPTxGNAgxL (x: unidentified, g: weakly assigned glycine) which corresponds to the residues 18-29 of the putative precursor.

摘要

我们通过蛋白质测序鉴定出新生大鼠脑中β蛋白的前体。针对与假定的β-淀粉样蛋白前体的羧基末端30个残基(666 - 695)相对应的合成肽制备了兔抗体(Kang等人,1987年)。该抗血清在新生大鼠脑匀浆的Triton X - 100提取物印迹中识别出110 - 130 kD的多条带。将部分纯化的免疫反应性蛋白进行SDS - PAGE,电泳转移到聚偏二氟乙烯膜上,并分析其部分氨基末端序列。三种主要的免疫反应性多肽中的每一种都产生了相同的氨基末端序列LEVPTxGNAgxL(x:未鉴定,g:弱分配的甘氨酸),该序列对应于假定前体的18 - 29位残基。

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