Abstract
Abstract: A rapid and efficient immunoaffinity purification procedure has been developed for human placental choline acetyltransferase (ChAT). Using this procedure, human placental ChAT was purified to homogeneity with high recovery of enzyme activity (50–60%). Purified ChAT was used to raise a monospecific anti‐human ChAT polyclonal antibody in rabbits. A comparison of the physical properties of ChAT was made between the enzymes purified from human brain and human placenta. Only one form of the enzyme exists in either tissue, having identical molecular weights of 68,000 and a single apparent pI of 8.1. A more detailed comparison of the two enzymes using peptide mapping and epitope mapping indicates identity between the brain and placental enzymes.
Original language | English (US) |
---|---|
Pages (from-to) | 611-620 |
Number of pages | 10 |
Journal | Journal of Neurochemistry |
Volume | 45 |
Issue number | 2 |
DOIs | |
State | Published - Aug 1985 |
Keywords
- Choline acetyltransferase
- Immunoaffinity purification
- Polyclonal choline acetyltransferase antibody
ASJC Scopus subject areas
- Biochemistry
- Cellular and Molecular Neuroscience