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Choline Acetyltransferase Staining in Brain Sections
Cold Spring Harbor Protocols, 2010INTRODUCTIONThis protocol describes the use of immunocytochemical methods to stain for choline acetyltransferase (ChAT). The avidin-biotin horseradish peroxidase complex (ABC) triple-labeling method used here takes advantage of the extraordinary affinity between avidin and biotin.
Carol Ann, Paul +2 more
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Activation of Choline Acetyltransferase by Salts
Nature New Biology, 1971IONIZED salts affect choline acetyltransferase, EC 2.3.1.6 (ChA), in two important ways. They change the equilibrium between soluble and membrane-bound ChA, in preparations of ruptured nerve endings1,2. Further, the rate of synthesis of acetylcholine by soluble ChA and the Michaelis constants for this reaction depend on the concentration of salts3. The
A K, Prince, E G, Hide
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Choline Acetyltransferase Activity in Omental Tissue
British Journal of Neurosurgery, 1987Choline acetyltransferase (ChAT), the enzyme responsible for the formation of ACh from choline and acetyl-coenzyme A, is a marker of cholinergic function and is significantly depressed in the brains of Alzheimer patients. It has been shown that omental tissue contains several neuroactive substances and causes revascularization when placed upon the ...
H S, Goldsmith, J K, Marquis, G, Siek
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Purification of chicken brain choline acetyltransferase
Neurochemistry International, 1981Chicken brain choline acetyltransferase was purified to homogeneity using ammonium sulfate fractionation, followed by chromatography on DEAE-Sephadex (A-25), hydroxyapatite, Sephadex G-150, immunoabsorption and Sepharose-CoA columns. A purification of 3500-fold was achieved and the final preparation had a specific activity of 2:32 ?mol acetylcholine ...
J H, Peng, K, Ma, S C, Sung
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Choline acetyltransferase: Purification and characterization
Journal of Neuroscience Research, 1980AbstractCholine acetyltransferase catalyzes the synthesis of the neurotransmitter acetylcholine and is the specific enzyme marker for cholinergic neurons. This review summarizes and discusses different purification procedures, as well as the characteristics of this important enzyme.
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Choline Acetyltransferase in Bovine Pineal Gland
Journal of Pineal Research, 1990Recent studies from our laboratories have shown that the bovine pineal gland contains a muscarinic cholinergic receptor with a Kd value of 0.423 ± 0.010 nM and a Bmax value of 69.75 ± 20.91 fmol/mg protein. In order to substantiate further the possible existence of a pineal cholinergic transmission, we have measured the activity of choline ...
P, Phansuwan-Pujito +2 more
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Choline Acetyltransferase: Celebrating Its Fiftieth Year
Journal of Neurochemistry, 1994Abstract: It is well known that the regulation of choline acetyltransferase (ChAT) activity under physiological and pathological conditions is important for the development and neuronal activities of cholinergic systems involved in many fundamental brain functions.
D, Wu, L B, Hersh
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Choline acetyltransferase in the snail brain
Comparative and General Pharmacology, 1970Abstract 1. 1. Choline acetyltransferase was detected and measured in Helix pomatia suboesophageal ganglia. 2. 2. The highest level of activity was observed at 35°C. and p H 7·5.
G A, Cottrell, B, Powell
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Drosophila Choline Acetyltransferase Temperature-Sensitive Mutants
Neurochemical Research, 1999We used the reverse transcription-polymerase chain reaction (RT-PCR) to amplify choline acetyltransferase (ChAT) mRNA fragments from two temperature-sensitive alleles of Drosophila melanogaster, Cha(ts1) and Cha(ts2). Single base substitutions in the mutants (T1614A in Cha(ts1) and G1596A in Cha(ts2)) would result in amino acid changes for ChAT protein
W, Wang, T, Kitamoto, P M, Salvaterra
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Carrier-mediated inhibition of choline acetyltransferase
Life Sciences, 1980Abstract Incubation of rat forebrain synaptosomes with choline mustard aziridinium ion in a sodium-rich medium caused a time-dependent inhibition of the high-affinity transport of choline, as well as a significant decrease in intrasynaptosomal choline acetyltransferase activity.
B J, Rylett, E H, Colhoun
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