High-yield purification of fetal tau preserving its structure and phosphorylation pattern

Journal of Immunological Methods
Natalia IvanovovaMichal Novak

Abstract

The fetal type of tau phosphorylation always re-appears during pathogenesis of Alzheimer's disease and related tauopathies. The major obstacle in the study of the fetal tau phosphorylation has been the lack of a simple and reproducible purification method yielding fetal tau with high purity and unmodified phosphorylation pattern. We have developed a two-step, highly efficient purification procedure of perchloric acid-extracted fetal tau by immunoaffinity chromatography and trichloroacetic acid (TCA) precipitation. The method yielded tau with more than 90% purity. Most importantly, purified fetal tau exhibited unmodified phosphorylation pattern as confirmed by phosphorylation-dependent antibodies. In summary, this purification process preserves and protects unstable phosphoresidues from dephosphorylation and allows their detailed molecular analysis especially in the pathogenesis of Alzheimer's disease and related tauopathies.

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Citations

Feb 20, 2009·Cellular and Molecular Neurobiology·Branislav KovacechMichal Novak
Sep 26, 2017·Biochemical and Biophysical Research Communications·Taiki ShimizuTakafumi Uchida

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