The calpain-induced proteolysis of tau associated with twice-cycled microtubules or from a total brain heat-stable fraction was studied. Twice-cycled microtubule tau was rapidly hydrolyzed by calpain. In contrast, tau purified from the total brain heat-stable fraction was very resistant to degradation by calpain. These results clearly demonstrate that there are at least 2 populations of tau in the brain based on calpain-sensitivity, a calpain-sensitive form that is associated with microtubules and a calpain-resistant form that may represent another population of tau in the brain.
|Original language||English (US)|
|Number of pages||7|
|Journal||Biochemical and biophysical research communications|
|State||Published - Sep 29 1989|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology