[HTML][HTML] Nonsaturable binding indicates clustering of tau on the microtubule surface in a paired helical filament-like conformation
M Ackmann, H Wiech, E Mandelkow - Journal of Biological Chemistry, 2000 - ASBMB
Tau protein modulates microtubule dynamics and forms insoluble aggregates in Alzheimer's
disease. Because there is a discrepancy between reported affinities of Tau to microtubules,
we determined the interaction over a wide concentration range using a sensitive enzyme-
linked immunosorbent assay. We found that the interaction is biphasic and not monophasic
as assumed earlier. The first binding phase is typical for identical and noninteracting binding
sites, with dissociation constants around 0.1 μmand stoichiometries around 0.2 Tau/tubulin …
disease. Because there is a discrepancy between reported affinities of Tau to microtubules,
we determined the interaction over a wide concentration range using a sensitive enzyme-
linked immunosorbent assay. We found that the interaction is biphasic and not monophasic
as assumed earlier. The first binding phase is typical for identical and noninteracting binding
sites, with dissociation constants around 0.1 μmand stoichiometries around 0.2 Tau/tubulin …