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Cellular localization of the molecular forms of acetylcholinesterase in rat diaphragm.

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This article is published in Journal of Biological Chemistry.The article was published on 1982-11-25 and is currently open access. It has received 162 citations till now. The article focuses on the topics: Diaphragm (structural system) & Cellular localization.

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Citations
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Journal ArticleDOI

Molecular and cellular biology of cholinesterases

TL;DR: In this article, the authors propose a method to identify the root cause of a problem.Abbreviations: [2]... ].., [3]
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Human endplate acetylcholinesterase deficiency caused by mutations in the collagen-like tail subunit (ColQ) of the asymmetric enzyme

TL;DR: Cloned human COLQ cDNA was cloned, the genomic structure and chromosomal localization of COLQ was determined, and mutations in this gene were identified in six patients with disabling congenital myasthenic syndrome, EP AChE deficiency.
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Isolation and characterization of acetylcholinesterase from Drosophila.

TL;DR: The purification and characterization of acetylcholinesterase from heads of the fruit fly Drosophila and the hydrolyzed butyrylthiocholine much more efficiently than these eel or human enzymes are described, an indication that the fly head enzyme has a substrate specificity intermediate between mammalian acetyl Cholinestersterases and butyRYlchlinesterases.
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Acetylcholinesterase from bovine caudate nucleus is attached to membranes by a novel subunit distinct from those of acetylcholinesterases in other tissues.

TL;DR: Quantitative gel slicing of 3H- and 125I-labeled nonreduced enzyme supported a structural model in which the tetrameric enzyme is a dimer of nonidentical catalytic subunit dimers, one of which involves a direct intersubunit disulfide linkage between two 70-kDa catalyticSubunit monomers and the second of which contains two disulfides linkages through an intervening 125I
References
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Journal ArticleDOI

A rapid, simple radiometric assay for cholinesterase, suitable for multiple determinations

TL;DR: A rapid and simple radiometric assay for cholinesterase, suitable for multiple determinations, has been developed, highly reproducible, quite sensitive, and useful for applications in which multiple samples must be quickly assayed.
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Multiple forms of acetylcholinesterase and their distribution in endplate and non-endplate regions of rat diaphragm muscle.

TL;DR: Although the activity of all three forms of acetylcholinesterase were decreased in denervated muscle, the largest proportional decrease occurred in theActivity of the 16 S form, which may correspond to the endplate enzyme.
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Cholinesterase is associated with the basal lamina at the neuromuscular junction

TL;DR: Direct evidence is presented that junctional ChE is associated with the basal lamina of the synaptic cleft in skeletal muscle, a protein known to be a principal component of BLs.
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Asymmetric and globular forms of acetylcholinesterase in mammals and birds.

TL;DR: The nomenclature introduced is very probably valid for the main AcChoE molecular forms, at least in vertebrates, and should help to clarify structural relationships and homologies among them, and does not claim to represent entirely the complex polymorphism of Ac ChoE.
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Enzymatic Detachment of Endplate Acetylcholinesterase from Muscle

TL;DR: It is reported here that enzymatic treatment of intact muscle causes the detachment of active endplate acetylcholinesterase from the muscle into the bathing fluid.
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