Results 141 to 150 of about 19,005 (175)
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Journal of Neurochemistry, 1981
Abstract: The choline analog homocholine is not acetylated in vitro by choline‐O‐acetyltransferase (ChAT, EC 2.3.1.6), which is solubilized by 100 mM‐sodium phosphate buffer washes of a crude vesicular fraction of mouse forebrain. However, both homocholine and choline are acetylated by a form of ChAT which is nonionically associated with a subcellular
C G, Benishin, P T, Carroll
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Abstract: The choline analog homocholine is not acetylated in vitro by choline‐O‐acetyltransferase (ChAT, EC 2.3.1.6), which is solubilized by 100 mM‐sodium phosphate buffer washes of a crude vesicular fraction of mouse forebrain. However, both homocholine and choline are acetylated by a form of ChAT which is nonionically associated with a subcellular
C G, Benishin, P T, Carroll
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Journal of Neurochemistry, 1983
Abstract: Three forms of acetyl coenzyme A: choline‐O‐acetyltransferase (EC 2.3.1.6, ChAT) have been isolated from mouse and rat forebrain synaptosomes with a 100 mM sodium phosphate (NaP) buffer of pH 7.4, a high‐salt solution (500 mM NaCl), and a 2% Triton DN‐65 solution, respectively.
C G, Benishin, P T, Carroll
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Abstract: Three forms of acetyl coenzyme A: choline‐O‐acetyltransferase (EC 2.3.1.6, ChAT) have been isolated from mouse and rat forebrain synaptosomes with a 100 mM sodium phosphate (NaP) buffer of pH 7.4, a high‐salt solution (500 mM NaCl), and a 2% Triton DN‐65 solution, respectively.
C G, Benishin, P T, Carroll
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Brain Research, 1994
Some of the choline-O-acetyltransferase (EC 2.3.1.6; ChAT) in rat hippocampal nerve terminals is non-ionically associated with membranes. The intent of the present report was to ascertain whether any of this membrane-bound ChAT might be associated with synaptic vesicles.
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Some of the choline-O-acetyltransferase (EC 2.3.1.6; ChAT) in rat hippocampal nerve terminals is non-ionically associated with membranes. The intent of the present report was to ascertain whether any of this membrane-bound ChAT might be associated with synaptic vesicles.
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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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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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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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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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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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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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