Proteolytic digestion patterns of "soluble" and "detergent-soluble" bovine caudate nucleus acetylcholinesterases.
The structures of purified "soluble" and "detergent-soluble" bovine caudate nucleus acetylcholinesterases were compared by peptide mapping on polyacrylamide gels. The digestion products generated from the two acetylcholinesterases on proteolysis by a given protease (Staphylococcus aureus V8 protease, alpha-chymotrypsin, or papain) are remarkably similar as judged from the electrophoretic band patterns. We conclude that the "soluble" and "detergent-soluble" acetylcholinesterases from bovine caudate nucleus share a common evolutionary origin.
D000110:Acetylcholinesterase / Q000032:analysis*; D000818:Animals; D002417:Cattle; D002421:Caudate Nucleus / Q000201:enzymology*; D003902:Detergents; D008565:Membrane Proteins / Q000032:analysis; D010446:Peptide Fragments / Q000032:analysis; D012995:Solubility
D003902:Detergents; D008565:Membrane Proteins; D010446:Peptide Fragments; D000110:Acetylcholinesterase