Human acetylcholinesterase. Immunochemical studies with monoclonal antibodies

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Monoclonal antibodies were used to investigate the immunochemistry of human erythrocyte acetylcholinesterase (acetylcholine acetylhydrolase, EC 3.1.1.7.). A series of experiments on the sedimentation velocity and Stokes radius of acetylcholinesterase and its immune complexes indicated that each antibody recognized a single high-affinity binding site (epitope) on the monomeric enzyme. Further analysis suggested that the antibody-binding sites were replicated on multimeric enzyme forms but were subject to steric hindrance between nearby IgG molecules or adjacent enzyme subunits. The cellular localization of the epitopes was studied by measuring the binding of monoclonal antibodies to the cholinesterase of intact erythrocytes. The results implied that most of the epitopes are exposed to the external media. However, one antibody failed to bind to intact cells, despite a relatively high affinity for detergent-solubilized antigen, possibly because its epitope is buried in the lipid bilayer.

Original languageEnglish (US)
Pages (from-to)290-297
Number of pages8
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume828
Issue number3
DOIs
StatePublished - Apr 29 1985

Fingerprint

Acetylcholinesterase
Epitopes
Monoclonal Antibodies
Enzymes
Erythrocytes
Antibody Binding Sites
Immunochemistry
Lipid bilayers
Antibodies
Cholinesterases
Lipid Bilayers
Antigen-Antibody Complex
Sedimentation
Detergents
Immunoglobulin G
Binding Sites
Antigens
Molecules
Experiments

Keywords

  • (Human erythrocyte)
  • Acetylcholinesterase
  • Immunochemistry
  • Monoclonal antibody

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology
  • Structural Biology

Cite this

Human acetylcholinesterase. Immunochemical studies with monoclonal antibodies. / Brimijoin, William Stephen; Mintz, Keith P.

In: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, Vol. 828, No. 3, 29.04.1985, p. 290-297.

Research output: Contribution to journalArticle

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