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Characterization of Choline O-Acetyltransferase (ChAT) in the BALB/C Mouse Spleen

International Journal of Neuroscience, 1994
The synthesizing enzyme, Choline-O-acetyl transferase (ChAT) (EC 2.3.1.6) and the degradation enzyme, acetylcholinesterase (EC 3.1.1.7) for the neurotransmitter acetylcholine, have been anatomically and biochemically characterized in the thymus of the BALB/C mouse.
K, Bulloch, T, Damavandy, M, Badamchian
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Combined pharmacological and fine-structural studies of choline O-acetyltransferase at the myoneural junction

Brain Research, 1977
Summary A cytochemical method for the fine-structural localization of choline-O-acetyltransferase (ChAc, EC 2.3.1.6) at newt myoneural junctions has been developed. Experiments were controlled by biochemical justification of each procedure. Triceps muscles were fixed in 2% buffered formaldehyde, washed and incubated with choline, acetyl coenzyme A ...
M E, Feigenson, R J, Barrnett
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Immunochemical Studies of Bovine and Human Choline‐O‐Acetyltransferase Using Monoclonal Antibodie

Journal of Neurochemistry, 1982
Abstract: Immunochemical properties of bovine and human choline acetyltransferase (ChAT, EC 2.3.1.6, acetyl‐CoA:choline‐O‐acetyltransferase) were studied using six monoclonal antibodies (AB1, AB5, AB6, AB7, AB8, and AB9) reactive with the enzyme. All antibodies except AB1 bound specifically to two proteins of 68,000 and 70,000 MW on “Western” blots of
A I, Levey, D B, Rye, B H, Wainer
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Amphiphilic and hydrophilic forms of choline-O-acetyltransferase in cholinergic nerve endings of the Torpedo

Neuroscience, 1986
In the purely cholinergic nerve endings isolated (i.e. synaptosomes) from the electric organ of the fish Torpedo, the enzyme choline acetyltransferase was found to exist not solely in its well-known soluble form but also in a form which is non-ionically bound to the plasma membrane; this activity could not be solubilized in solutions of high ionic ...
L, Eder-Colli, S, Amato, Y, Froment
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Membrane-bound choline-O-acetyltransferase in rat hippocampal tissue is anchored by glycosyl-phosphatidylinositol

Brain Research, 1993
In an earlier study, we presented evidence to suggest that some of the particulate choline-O-acetyltransferase (ChAT) in rat hippocampal tissue might be linked to membranes by a glycosyl-phosphatidylinositol (GPI) anchor. In the present report, we attempted to determine if any of this GPI-anchored ChAT might be intracellular.
L K, Smith, P T, Carroll
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Genetic variation in the choline O-acetyltransferase gene in depression and Alzheimer’s disease: The VITA and Milano studies

Journal of Psychiatric Research, 2011
Linkage studies point to the long arm of chromosome 10 being a susceptibility region for Alzheimer's disease (AD). Additionally, the gene choline O-acetyltransferase (CHAT) located on chromosome 10 was discussed for conveying risk towards AD, but the results are ambiguous.
E. Grünblatt   +14 more
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Organization of central cholinergic neurons revealed by combined in situ hybridization histochemistry and choline-O-acetyltransferase immunocytochemistry

Neurochemistry International, 1992
Digoxigenin-labeled riboprobes and in situ hybridization of choline-O-acetyltransferase mRNA, both alone and in combination with immunohistochemical procedures for the synthetic enzyme of acetylcholine, were used to map the topography of putative cholinergic neurons in the rat central nervous system.
L L, Butcher   +4 more
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A comparison of solubilized and membrane bound forms of choline-O-acetyltransferase (EC 2.3.1.6) in mouse brain nerve endings

Brain Research, 1980
Abstract Mouse brain choline-O-acetyltransferase (EC 2.3.1.6) (ChAT) activity was studied in vitro using a 100 mM sodium phosphate buffer (pH 7.4) wash of a crude vesicular fraction containing solubilized ChAT and a washed crude vesicular fraction containing membrane bound ChAT.
C P, Smith, P T, Carroll
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Veratridine-induced breakdown of cytosolic acetylcholine in rat hippocampal minces: An intraterminal form of acetylcholinesterase or choline O-acetyltransferase?

Brain Research, 1986
Rat hippocampal minces were loaded with N-methyl-[3H]acetylcholine ([3H]ACh) in the presence of the 'poorly penetrating' acetylcholinesterase (EC 3.1.1.7, AChE) inhibitor echothiophate and the effect of the depolarizing agent veratridine determined on the subcellular storage and release of [3H]ACh and [3H]choline.
P T, Carroll   +3 more
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