Torpedo marmorata acetylcholinesterase; a comparison with the Electrophorus electricus enzyme. Molecular forms, subunits, electron microscopy, immunological relationship.
Electron microscopy, sequential degradation by hydrolytic enzymes and the physical-chemical properties of the molecular forms of Torpedo acetylcholinesterase indicate that these molecules are structurally related to each other in the same way as the molecular forms of Electrophorus acetylcholinesterase: all are derived from a complex structure in which three tetrameric groups of subunits are associated with a rod-like 'tail'. In aged preparations the catalytic subunits are split into fragments in a manner similar to those of Electrophorus acetylcholinesterase. Immunological cross-reaction between both enzymes demonstrates the occurrence of common antigenic sites. The enzymes from the two sources, however, are different in their molecular weights and susceptibility to hydrolytic enzymes. Also, Torpedo acetylcholinesterase does not precipitate with either isologous or heterologous antibodies.
D000110:Acetylcholinesterase / Q000276:immunology; D000818:Animals; D003168:Complement Fixation Tests; D003429:Cross Reactions; D004237:Diuron; D004557:Electric Organ / Q000201:enzymology; D004593:Electrophorus; D000939:Epitopes; D005399:Fishes; D005779:Immunodiffusion; D007527:Isoenzymes / Q000276:immunology; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D011485:Protein Binding; D011487:Protein Conformation; D013045:Species Specificity
D000939:Epitopes; D007527:Isoenzymes; D046911:Macromolecular Substances; D010446:Peptide Fragments; D004237:Diuron; D000110:Acetylcholinesterase