Choline acetyltransferase (EC 18.104.22.168) catalyzes the biosynthesis of acetylcholine according to the following chemical equation: acetyl-CoA + choline in equilibrium to acetylcholine + CoA. In addition to nervous tissue, primate placenta is the only other animal source which contains appreciable acetylcholine and its biosynthetic enzyme. Human brain caudate nucleus and human placental choline acetyltransferase were purified to electrophoretic homogeneity using ion-exchange and blue dextran-Sepharose affinity chromatography. The molecular weights determined by Sephadex G-150 gel filtration and sodium dodecyl sulfate gel electrophoresis are 67000 plus or minus 3000. N-Ethylmaleimide, p-chloromercuribenzoate, and dithiobis(2-nitrobenzoic acid) inhibit the enzyme. Dithiothreitol reverses the inhibition produced by the latter two reagents. The pKa of the group associated with N-ethylmaleimide inhibition is 8.6 plus or minus 0.3. A chemically competent acetyl-thioenzyme is isolable by Sephadex gel filtration. The enzymes from the brain and placenta are thus far physically and biochemically indistinguishable.
A complementary DNA for human choline acetyltransferase induces two forms of enzyme with different molecular weights in cultured cells
Translation initiation sites and relative activity of large and small forms of human choline acetyltransferase
Specific antibodies to bovine choline acetyltransferase raised in mice immunised with small amounts of partially purified enzyme
Immunization of guinea pigs with human choline acetyltransferase induces selective lower motoneuron destruction
Preparation of antibodies specific to choline acetyltransferase from bovine caudate nucleus and immunohistochemical localization of the enzyme
A fluorometric assay for choline acetyltransferase and its use in the purification of the enzyme from human placenta
Molecular characterization of choline acetyltransferase from bovine brain caudate nucleus and some immunological properties of the highly purified enzyme
Functional analysis of conserved histidines in choline acetyltransferase by site-directed mutagenesis
Acceleration of choline uptake after depolarization-induced acetylcholine release in rat cortical synaptosomes
Anti-human choline acetyltransferase fragments antigen binding (FAB)-sepharose chromatography for enzyme purification
Highly sensitive assay for choline acetyltransferase activity by high-performance liquid chromatography with electrochemical detection
Relationships between chemical structure and inhibition of human placental choline acetyltransferase by keto analogs of acetylcholine
Properties and partial purification of choline acetyltransferase from the nematode Caenorhabditis elegans
Immunoaffinity purification of human choline acetyltransferase: comparison of the brain and placental enzymes
Health Span-Extending Activity of Human Amniotic Membrane- and Adipose Tissue-Derived Stem Cells in F344 Rats
Identification of an active site arginine in rat choline acetyltransferase by alanine scanning mutagenesis.
Basal Ganglia are a group of subcortical nuclei in the brain associated with control of voluntary motor movements, procedural and habit learning, emotion, and cognition. Here is the latest research.