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Identification of a 17 S asymmetric butyrylcholinesterase in chick muscle by monoclonal antibodies

Authors
Journal
Neuroscience Letters
0304-3940
Publisher
Elsevier
Publication Date
Volume
86
Issue
2
Identifiers
DOI: 10.1016/0304-3940(88)90579-4
Keywords
  • Acetylcholinesterase
  • Butyrylcholinesterase
  • Monoclonal Antibody
  • Chick Muscle
  • Collagenous Tail
Disciplines
  • Biology

Abstract

Abstract A 20 S asymmetric (non-globular) form of acetylcholinesterase (AChE, E.C. 3.1.1.7) has been purified from 1-day chick muscle. This form is a hybrid molecule containing both AChE and butyrylcholinesterase (BuChE, E.C. 3.1.1.8) catalytic subunits, linked through a collagenous tail. However, the 20 S hybrid AChE/BuChE could not account for the total enzyme activities of AChE and BuChE in a high-salt/Triton X-100 extract of 1-day chick muscle. By applying AChE- and BuChE-specific monoclonal antibodies for immunoadsorption, homogeneous asymmetric AChE and BuChE forms were also identified in that extract. The homogeneous BuChE accounts for 20% of the total activity of the asymmetric BuChE present and sediments at 17 S. About 6% of the asymmetric AChE present is, likewise, in a homogeneous, instead of the hybrid, form. The 17 S asymmetric BuChE does not react with monoclonal antibodies specific for the collagenous tail of the hybrid 20 S AChE/BuChE molecule, suggesting that the collagenous subunit differs between these two forms.

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