منابع مشابه
Choline acetyltransferase from rat brain.
The localization, purification, and some enzymatic properties of choline acetyltransferase from rat brain were studied. Most assays were performed with a specific radiometric micromethod. Solubilization of the enzyme was examined after homogenization of cerebral cortices by means which disintegrate nerve endings. In isotonic KC1 the enzyme was recovered in solution. In more dilute KC1 the enzym...
متن کاملCholine transporter 1 maintains cholinergic function in choline acetyltransferase haploinsufficiency.
Choline acetyltransferase (ChAT), the enzyme that synthesizes the neurotransmitter acetylcholine (ACh), is thought to be present in kinetic excess in cholinergic neurons. The rate-limiting factor in ACh production is the provision of choline to ChAT. Cholinergic neurons are relatively unique in their expression of the choline transporter 1 (CHT1), which exhibits high-affinity for choline and ca...
متن کاملCholine acetyltransferase. Inhibition by thiol reagents.
Choline acetyltransferase (EC 2.3.1.6) catalyzes the reversible transfer of the acetyl group from acetyl coenzyme A to choline. Previous studies are consistent with the idea that an active site sulfhydryl group reacts with acetyl coenzyme A to form an acetyl-thioenzyme intermediate and coenzyme A (ROSKOSKI, R., JR. (1973) Biochemistry 12, 3709). Choline then reacts with the acetyl-enzyme to for...
متن کاملCloning of Drosophila choline acetyltransferase cDNA.
Choline acetyltransferase (EC 2.3.1.6) is the biosynthetic enzyme for the neurotransmitter acetylcholine. To isolate choline acetyltransferase cDNA clones, a cDNA library was constructed from poly(A)+ RNA of Drosophila melanogaster heads, these being one of the richest known sources of the enzyme. By screening the cDNA library with a mixture of three different monoclonal antibodies to Drosophil...
متن کاملThe choline acetyltransferase of human placenta.
1. Various methods for the extraction of choline acetyltransferase (acetyl-CoA-choline O-acetyltransferase, EC 2.3.1.6) from immature human placenta (18-28 weeks of gestation) are described. 2. The crude enzyme was found to be stable at -18 degrees and +4 degrees under a variety of conditions. 3. Purification methods, including ammonium sulphate fractionation, gel filtration on various grades o...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1974
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)42811-1