Human brain and placental choline acetyltransferase: purification and properties.

@article{Roskoski1975HumanBA,
  title={Human brain and placental choline acetyltransferase: purification and properties.},
  author={Robert Roskoski and C. T. Lim and Laura M. Roskoski},
  journal={Biochemistry},
  year={1975},
  volume={14 23},
  pages={
          5105-10
        }
}
Choline acetyltransferase (EC 2.3.1.6) 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… 
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Physical and Kinetic Properties of Choline Acetyl Transferase from Rat and Bovine Brain
TLDR
Initial velocity studies for both enzymes indicated a sequential mechanism, in which both substrates must bind before either product is released, and product inhibition studies with the rat enzyme showed that acetylcholine was competitive withrespect to choline, and noncompetitive with respect to acetyl‐CoA, while CoA inhibited competitively with respectto acetyl-CoA and non Competitively with Respect to Choline.
Studies on choline acetyltransferase isolated from human brain
TLDR
The purified choline acetyltransferase from human striatal tissue was found to have aKm value of 8μM for acetyl-coenzyme A and 250 μM for choline, and this activity was enhanced 2- to 3-fold by KCl, NaCl, (NH4)2SO4, and chelating agents like EDTA or EGTA, but not by the substrates, histidine, or imidazole.
MOLECULAR CHARACTERIZATION OF CHOLINE ACETYLTRANSFERASE FROM BOVINE BRAIN CAUDATE NUCLEUS AND SOME IMMUNOLOGICAL PROPERTIES OF THE HIGHLY PURIFIED ENZYME
TLDR
The results of binding studies with affinity columns, suggest that the enzyme contains a hydrophobic lobe and a dinucleotide fold, and that a free purine rather than a free ribosyl ring of acetyl‐CoA is important for the binding of the substrate to the active site.
Purification and immunochemical properties of choline acetyltransferase from human brain
Choline acetyltransferase (CAT) was purified to homogeneity from 363 g of human neostriatum by means of ammonium sulfate and protamine sulfate fractionation, followed by chromatography on…
Choline acetyltransferase
  • L. Chao
  • Biology, Chemistry
    Neurochemical Research
  • 2004
No multiple forms of choline acetyltransferase were found in extracts of human, mouse, rabbit, guinea pig, cat, and rat brain. A single form of this enzyme only was also demonstrated in bovine…
Choline acetyltransferase aggregates from human placenta and rat brain
Purification and Some Properties of Choline Acetyltransferase from Catfish Brain
TLDR
Double immunodiffusion test with CAT antibodies and a crude enzyme extract from catfish brains showed only a single, sharp precipitin band, suggesting that the antibodies are specific only to CAT and antigen and that the purified CAT preparation is monodisperse.
Relationships between chemical structure and inhibition of human placental choline acetyltransferase by keto analogs of acetylcholine.
TLDR
The most potent and selective inhibitor of choline acetyltransferase was (2-benzoylethyl)trimethylammonium chloride with an I50 of 3 X 10(-6) M.
Production of specific antibodies to choline acetyltransferase purified from pig brain
Immunoaffinity Purification of Human Choline Acetyltransferase: Comparison of the Brain and Placental Enzymes
TLDR
Using this procedure, human placental ChAT was purified to homogeneity with high recovery of enzyme activity (50–60%) and was used to raise a monospecific anti‐human ChAT polyclonal antibody in rabbits.
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References

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TLDR
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