Isoelectric point differentiates PHF-tau from biopsy-derived human brain tau proteins.
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.
Sergeant
N
N
Unité INSERM 422, Lille, France.
Bussière
T
T
Vermersch
P
P
Lejeune
J P
JP
Delacourte
A
A
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*
D016900:Neurofilament Proteins; D016875:tau Proteins