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Isoelectric point differentiates PHF-tau from biopsy-derived human brain tau proteins

1995; Lippincott Williams & Wilkins; Volume: 6; Issue: 16 Linguagem: Inglês

10.1097/00001756-199511000-00028

1473-558X

Nicolas Sergeant, Thierry Bussière, Patrick Vermersch, Julien Lejeune, A. Delacourte,

Protein Structure and Dynamics

IN the present study, Tau proteins were detected by two monoclonal antibodies AD2 and Tau-1 raised against PHF-tau and normal Tau proteins respectively using single- and two-dimensional immunoblotting. We demonstrate here the presence of a Tau triplet in brain homogenates from patients with Alzheimer's disease (AD) processed human brain biopsies from controls. However PHF-tau proteins have a slight but significantly higher mol. wt and a much more acidic isoelectric point. Therefore, Tau proteins are more phosphorylated in AD.