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

被引：38

作者：

SERGEANT, N

BUSSIERE, T

VERMERSCH, P

LEJEUNE, JP

DELACOURTE, A

机构：

[1] INSERM,U422,F-59045 LILLE,FRANCE

[2] CHU LILLE,NEUROCHIRURG CLIN,F-59037 LILLE,FRANCE

来源：

NEUROREPORT | 1995年 / 6卷 / 16期

关键词：

ALZHEIMERS DISEASE; PHF-TAU; NEUROFIBRILLARY DEGENERATION; PHOSPHORYLATION; MONOCLONAL ANTIBODIES; WESTERN BLOTS; 2-DIMENSIONAL GEL ELECTROPHORESIS;

D O I：

10.1097/00001756-199511000-00028

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

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.

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页码：2217 / 2220

页数：4

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