Results 141 to 150 of about 14,687,166 (179)
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Immunochemical Studies of Bovine and Human Choline‐O‐Acetyltransferase Using Monoclonal Antibodie
Journal of Neurochemistry, 1982Abstract: 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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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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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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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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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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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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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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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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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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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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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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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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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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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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