title: Isoelectric point differentiates PHF-tau from biopsy-derived human brain tau proteins.
abstract: 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.
authors.affiliation: Unité INSERM 422, Lille, France.
authors.forename: N
authors.initials: N
authors.lastname: Sergeant
authors.forename: T
authors.initials: T
authors.lastname: Bussière
authors.forename: P
authors.initials: P
authors.lastname: Vermersch
authors.forename: J P
authors.initials: JP
authors.lastname: Lejeune
authors.forename: A
authors.initials: A
authors.lastname: Delacourte
mesh_terms: D000328:Adult; D001706:Biopsy; D001923:Brain Chemistry / Q000502:physiology*; D006801:Humans; D015151:Immunoblotting; D007526:Isoelectric Point; D008875:Middle Aged; D016874:Neurofibrillary Tangles / Q000737:chemistry*; D016900:Neurofilament Proteins / Q000737:chemistry*; D016875:tau Proteins / Q000737:chemistry*
chemical_list: D016900:Neurofilament Proteins; D016875:tau Proteins