Kondo J, Honda T, Mori H, Hamada Y, Miura R, Ogawara M, Ihara Y
Mitsubishi Kasei Corporation Research Center, Biosciences Laboratory, Yokohama, Japan.
Neuron. 1988 Nov;1(9):827-34. doi: 10.1016/0896-6273(88)90130-4.
To obtain definitive evidence that tau is a component of paired helical filaments (PHF) in Alzheimer's disease, we fractionated and sequenced PHF-derived peptides according to a previously described procedure. In the PHF digest, we found four independent tau peptides that were located in the carboxyl third of tau. Subsequent extensive analysis of the PHF digest did not provide any other tau peptides. The conventional PHF antiserum and a new antiserum directed toward formic acid-denatured PHF reacted with the distinct CNBr fragments of tau localized on the carboxy-terminal portion of tau by protein sequencing. From these observations, we conclude that the carboxyl third of tau is tightly bound to PHF.
为了获得确凿证据证明tau是阿尔茨海默病中双螺旋丝（PHF）的一个组成部分，我们按照先前描述的程序对源自PHF的肽进行了分级分离和测序。在PHF消化物中，我们发现了四个独立的tau肽，它们位于tau的羧基端三分之一区域。随后对PHF消化物进行的广泛分析未发现任何其他tau肽。传统的PHF抗血清和一种针对甲酸变性PHF的新抗血清，通过蛋白质测序与tau的羧基末端部分上定位的tau的不同溴化氰片段发生反应。基于这些观察结果，我们得出结论，tau的羧基端三分之一区域与PHF紧密结合。
