ISOELECTRIC POINT DIFFERENTIATES PHF-TAU FROM BIOPSY-DERIVED HUMAN BRAIN TAU PROTEINS

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