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Title
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Primary structure of Torpedo californica acetylcholinesterase deduced from its cDNA sequence.
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Authors
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M.Schumacher,
S.Camp,
Y.Maulet,
M.Newton,
K.MacPhee-Quigley,
S.S.Taylor,
T.Friedmann,
P.Taylor.
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Ref.
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Nature, 1986,
319,
407-409.
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PubMed id
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Abstract
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Acetylcholinesterase, an essential enzyme of the nervous system, rapidly
terminates the action of acetylcholine released into the synapse.
Acetylcholinesterase is also found (in lower abundance) in extrajunctional areas
of muscle and nerve and on erythrocyte membranes. Hydrodynamic analyses of the
native enzyme and characterization of its dissociated subunits have revealed
multiple enzyme forms which can be divided into two classes: dimensionally
asymmetric forms which are usually found within the synapse and contain a
collagen-like structural subunit disulphide-linked to the catalytic subunits;
and globular forms which appear to be widely distributed on the outer surface of
cell membranes. Both forms have been characterized in the ray Torpedo
californica and, although their catalytic behaviours seem to be identical, they
differ slightly in amino-acid composition, peptide maps and reactivity with
certain monoclonal antibodies. Here, we report the complete amino-acid sequence
of an acetylcholinesterase inferred from the sequence of a complementary DNA
clone. The 575-residue protein shows significant homology with the C-terminal
portion of thyroglobulin.
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