Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1988-9-21
pubmed:abstractText
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-micrograms 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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0272-4340
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
85-93
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Monoclonal antibodies to human brain acetylcholinesterase: properties and applications.
pubmed:affiliation
Department of Pharmacology, Mayo Clinic, Rochester, Minnesota 55905.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.