Monoclonal antibodies to human brain acetylcholinesterase: properties and applications

Zoltan Rakonczay, Stephen Brimijoin

Research output: Contribution to journalArticle

22 Scopus citations

Abstract

1. Acetylcholinesterase (AChE) was purified 20,000-fold in a 43% yield from 90 g of human cerebellum by combined immunoaffinity and ligand affinity chromatography. The purified enzyme migrated as a 68,000-dalton band during polyacrylamide gel electrophoresis under denaturing and reducing conditions. 2. Balb/c mice were immunized with multiple 10-μg injections of this material in order to raise monoclonal antibodies to human brain AChE. Three such antibodies were obtained and characterized. 3. Each antibody cross-reacted distinctively with AChEs from other mammals. No antibody recognized human plasma butyrylcholinesterase but all reacted with AChE from human red blood cells. 4. Antibodies HR5 and HR3 performed well in two-site immunoassays for AChE. With these assays we compared autopsy samples of cortical region A9 from six controls (nonneurological cases) and five patients with Alzheimer's disease. The latter showed a highly significant 60% deficit of AChE protein. 5. The present antibodies will permit additional immunochemical studies of cholinergic systems in dementia.

Original languageEnglish (US)
Pages (from-to)85-93
Number of pages9
JournalCellular and molecular neurobiology
Volume8
Issue number1
DOIs
StatePublished - Mar 1 1988

Keywords

  • Alzheimer's disease
  • acetylcholinesterase
  • immunoassay

ASJC Scopus subject areas

  • Cellular and Molecular Neuroscience
  • Cell Biology

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