Results 151 to 160 of about 14,687,166 (179)
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Neurochemistry International, 1986
Choline-O-acetyltransferase (EC 2.3.1.6; ChAT) was prepared from synaptosomal fractions (P(2)) of mouse and rat brain in the presence of proteolytic inhibitors by the method of Gray and Whittaker (1962) as modified by (Salehmoghaddam and Collier, 1976).
M, Badamchian, K J, Morrow, P T, Carroll
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Choline-O-acetyltransferase (EC 2.3.1.6; ChAT) was prepared from synaptosomal fractions (P(2)) of mouse and rat brain in the presence of proteolytic inhibitors by the method of Gray and Whittaker (1962) as modified by (Salehmoghaddam and Collier, 1976).
M, Badamchian, K J, Morrow, P T, Carroll
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1986
The enzyme choline-o-acetyltransferase (EC 2.3.1.6; ChAT), which catalyses the biosynthesis of the neurotransmitter acetylcholine (ACh) from choline and acetylcoenzyme A (AcCoA), was traditionally thought to exist solely in a soluble form in the cytoplasm of cholinergic nerve endings.
L. Eder-Colli, S. Amato, Y. Froment
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The enzyme choline-o-acetyltransferase (EC 2.3.1.6; ChAT), which catalyses the biosynthesis of the neurotransmitter acetylcholine (ACh) from choline and acetylcoenzyme A (AcCoA), was traditionally thought to exist solely in a soluble form in the cytoplasm of cholinergic nerve endings.
L. Eder-Colli, S. Amato, Y. Froment
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Tissue and Cell
This experimental study aimed to investigate the role of SOX2OT in NT2 cell neuronal differentiation to elucidate its specific function in this process, which remains unclear despite previous research highlighting its importance in central nervous system development.We utilized the NT2 cell line to create a constitutive SOX2OT knocked-down cell clone ...
Marie, Saghaeian Jazi +3 more
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This experimental study aimed to investigate the role of SOX2OT in NT2 cell neuronal differentiation to elucidate its specific function in this process, which remains unclear despite previous research highlighting its importance in central nervous system development.We utilized the NT2 cell line to create a constitutive SOX2OT knocked-down cell clone ...
Marie, Saghaeian Jazi +3 more
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Journal of Neurochemistry, 1984
Abstract: Three fractions (one soluble and two membrane‐bound) of choline acetyltransferase (ChAT) isolated from a nerve ending fraction of mouse forebrain, which have previously been reported to differ in several biochemical and physical aspects, were also found to differ in their rates of postnatal development.
C G, Benishin, P T, Carroll
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Abstract: Three fractions (one soluble and two membrane‐bound) of choline acetyltransferase (ChAT) isolated from a nerve ending fraction of mouse forebrain, which have previously been reported to differ in several biochemical and physical aspects, were also found to differ in their rates of postnatal development.
C G, Benishin, P T, Carroll
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Brain Research, 1978
The present study compares choline acetylase (ChAc) activity with morphometric determinations of synaptic vesicles at the neuromuscular junctions of frog pectoralis muscle subjected to high and low frequency stimulation in the presence or absence of NVP, a ChAc inhibitor.
F M, Benes, R J, Barrnett
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The present study compares choline acetylase (ChAc) activity with morphometric determinations of synaptic vesicles at the neuromuscular junctions of frog pectoralis muscle subjected to high and low frequency stimulation in the presence or absence of NVP, a ChAc inhibitor.
F M, Benes, R J, Barrnett
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Journal of Neurochemistry, 1990
Abstract: Some of the enzyme choline‐O‐acetyltransferase (ChAT) associated with central cholinergic nerve terminals appears to be nonionically associated with membranes. In the present study, we tested the possibility that some membrane‐bound ChAT might be anchored to membranes by a phosphatidylinositol linkage by incubating rat hippocampal tissue ...
P T, Carroll, L K, Smith
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Abstract: Some of the enzyme choline‐O‐acetyltransferase (ChAT) associated with central cholinergic nerve terminals appears to be nonionically associated with membranes. In the present study, we tested the possibility that some membrane‐bound ChAT might be anchored to membranes by a phosphatidylinositol linkage by incubating rat hippocampal tissue ...
P T, Carroll, L K, Smith
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Brain Research, 1987
The effect of veratridine depolarization on the activity of 3 choline-O-acetyltransferase (ChAT) fractions in rat hippocampal tissue was investigated. Those concentrations of veratridine which augmented acetylcholine (ACh) release also increased the activity of water and detergent soluble ChAT fractions.
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The effect of veratridine depolarization on the activity of 3 choline-O-acetyltransferase (ChAT) fractions in rat hippocampal tissue was investigated. Those concentrations of veratridine which augmented acetylcholine (ACh) release also increased the activity of water and detergent soluble ChAT fractions.
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