Results 351 to 360 of about 218,218 (394)
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The phosphorylation of choline acetyltransferase

Neurochemical Research, 1989
Human placental Choline Acetyltransferase (ChAT) has been shown to be phosphorylated in vitro by kinases present in rat brain. Phosphorylation occurs at a single site with the exclusive phosphoamino acid being serine. ChAT phosphorylation was shown to be calcium, and not cyclic nucleotide, dependent and was inhibited by inhibitors of calcium/calmodulin
Louis B. Hersh, Gordon Bruce
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Histone acetyltransferase complexes

Seminars in Cell & Developmental Biology, 1999
Modification of histone amino terminal tails by acetylation has long been linked to the transcriptional capacity of genes in chromatin and to various aspects of chromatin dynamics. Over the last few years a flurry of reports have described the purification and identification of a large number of histone acetyltransferases.
Shelley L. Berger, Patrick A. Grant
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Acetyltransferases and susceptibility to chemicals

Toxicology Letters, 1992
Arylamine chemicals inflict a number of toxicities including cancer. Metabolic activation (i.e., oxidation) is required in order to elicit the toxic actions. Acetylation is an important step in the metabolic activation and deactivation of arylamines. N-acetylation forms the amide derivative which is often nontoxic.
Kyle D. Bucher   +7 more
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Choline acetyltransferase in schizophrenia

American Journal of Psychiatry, 1993
To test the hypothesis that schizophrenia involves altered cholinergic tone in the pons, the authors studied post-mortem brain tissue from subjects with schizophrenia.The authors used Western immunoblot to measure the concentration of choline acetyltransferase, an acetylcholine synthesizing enzyme, in the post-mortem brain tissue of 25 schizophrenic ...
C. N. Karson   +3 more
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ACETYLCHOLINE AND CHOLINE ACETYLTRANSFERASE

Neurochemistry International, 1980
The thermodynamics and kinetics of the alcoholysis of thiolesters are discussed and related to choline acetyltransferase. The conformation and rotational barriers of acetylcholine are described as is the specific inability of choline to induce depolarization. Evidence is presented for the involvement of imidazole and the non-involvement of thiol groups
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Regulation of Choline Acetyltransferase

1989
Publisher Summary This chapter presents the studies related to choline acetyltransferase (ChAT) and cholinergic biology into a more comprehensive neurobiological context. The recent results of biochemical, immunological, molecular biological, arid immunocytochemical studies of ChAT and its regulation are discussed.
J E Vaughn, P M Salvaterra
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Nomenclature for N-acetyltransferases

Pharmacogenetics, 1995
A consolidated classification system is described for prokaryotic and eukaryotic N-acetyltransferases in accordance with the international rules for gene nomenclature. The root symbol (NAT) specifically identifies the genes that code for the N-acetyltransferases, and NAT* loci encoding proteins with similar function are distinguished by Arabic numerals.
Kostas P. Vatsis   +12 more
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N-Acetyltransferases, O-Acetyltransferases, and N, O-Acetyltransferases: Enzymology and Bioactivation

1994
Publisher Summary Acetyltransferases play a central role in the metabolic disposition, detoxication, and bioactivation of a diverse group of drugs—carcinogens and other xenobiotics. Acetylation is a major metabolic pathway for primary aromatic amines (arylamines, ArNH) and hydrazines.
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Choline Acetyltransferase

CRC Critical Reviews in Biochemistry, 1977
Acetylcholine is essential to neural function. It synthesis is catalyzed by choline acetyltransferase, the enzyme responsible for the acetylation of choline by acetyl coenzye A, a reaction favored slightly thermodymodynamically and not at all kinetically. An analytically pure enzyme still has not been obtained; however, method of purification have been
Henry G. Mautner, David Nachmansohn
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Immunohistochemistry of Choline Acetyltransferase

1979
Publisher Summary This chapte discusses the problems related to immunohistochemistry of choline acetyltransferase (ChAT)-containing systems in the brain and spinal cord. The synthetic enzyme ChAT is a definitive marker for cholinergic neurons and their processes.
Patrick L. McGeer   +3 more
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