Abstract
A comparitive study was made of the enzyme choline acetyltransferase (ChAT) from normal and Alzheimer (senile dementia of the Alzheimer type) brain. The number of molecular weight and charge forms of the enzyme were determined in the caudate region of both brains. Efficient purification of active ChAT was achieved using immuno-affinity purification. It was shown that the purified enzyme was identical in both cases, exhibiting a single charge (apparent pI∼8.2) and a single molecular weight (mol. wt. = 68,000). The idea of a selective loss of one particular isoform to explain the reduced levels of ChAT observed in Alzheimer's disease can be ruled out.
Original language | English (US) |
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Pages (from-to) | 171-175 |
Number of pages | 5 |
Journal | Neuroscience letters |
Volume | 59 |
Issue number | 2 |
DOIs | |
State | Published - Aug 30 1985 |
Keywords
- Alzheimer's disease
- choline acetyltransferase
- multiple forms
ASJC Scopus subject areas
- Neuroscience(all)