| Literature DB >> 2551295 |
G V Johnson1, R S Jope, L I Binder.
Abstract
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.Mesh：
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Year: 1989 PMID： 2551295 DOI： 10.1016/0006-291x(89)91150-9
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575