The car☐yl third of tau is tightly bound to paired helical filaments

• Published in: Neuron (Cambridge, Mass.) Vol. 1; no. 9; pp. 827 - 834
• Main Authors: Kondo, Jun, Honda, Toshiyuki, Mori, Hiroshi, Hamada, Yoshio, Miura, Reiko, Ogawara, Midori, Ihara, Yasuo
• Format: Journal Article
• Language: English
• Published: Elsevier Inc 01.11.1988
• ISSN: 0896-6273; 1097-4199
• 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 car☐yl 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 car☐y-terminal portion of tau by protein sequencing. From these observations, we conclude that the car☐yl third of tau is tightly bound to PHF.