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阿尔茨海默病患者大脑微管和双螺旋丝中tau蛋白的特征分析。

Characterization of tau protein present in microtubules and paired helical filaments of Alzheimer's disease patient's brain.

作者信息

Nieto A, Montejo de Garcini E, Correas I, Avila J

机构信息

Centro de Biología Molecular (CSIC-UAM), Universidad Autónoma, Madrid, Spain.

出版信息

Neuroscience. 1990;37(1):163-70. doi: 10.1016/0306-4522(90)90201-e.

Abstract

Two proteins immunologically related to porcine tau protein are found in the brain of Alzheimer's disease patients. One is bound to microtubules and, after isolation by co-polymerization with tubulin, shows a size and tryptic peptide map, similar to the microtubule-associated tau protein, present in the brain of non-demented patients. The other tau-related protein is present as the major protein of a purified fraction of paired helical filaments. The paired helical filament-associated protein shows smaller molecular weight (33,000) than microtubule-associated tau; however, this 33,000 mol. wt protein reacts with a monospecific anti-tau antibody and with an antibody to a 19-amino acid peptide corresponding to amino acids 228-246 of human tau. Furthermore, the 33,000 mol. wt protein and the tau protein have similar tryptic peptide maps. These results suggest that the paired helical filament protein is a modified form of the microtubule-associated tau protein.

摘要

在阿尔茨海默病患者的大脑中发现了两种与猪tau蛋白存在免疫相关性的蛋白质。一种与微管结合,在通过与微管蛋白共聚合分离后,其大小和胰蛋白酶肽图与非痴呆患者大脑中存在的微管相关tau蛋白相似。另一种与tau相关的蛋白质是成对螺旋丝纯化组分中的主要蛋白质。成对螺旋丝相关蛋白的分子量(33,000)比微管相关tau蛋白小;然而,这种33,000道尔顿的蛋白质能与单特异性抗tau抗体以及针对对应于人tau蛋白第228 - 246位氨基酸的19氨基酸肽的抗体发生反应。此外,33,000道尔顿的蛋白质和tau蛋白具有相似的胰蛋白酶肽图。这些结果表明,成对螺旋丝蛋白是微管相关tau蛋白的一种修饰形式。

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