title: Molecular forms of purified human erythrocyte membrane acetylcholinesterase investigated by crosslinking with diimidates.
abstract: Several molecular forms of human erythrocyte membrane acetylcholinesterase have been studied after crosslinking with bifunctional diimidates. The crosslinked products were analysed by centrifugation on linear sucrose density gradients containing Triton X-100. Molecular weights of covalently linked oligomers were estimated by sodium dodecylsulfate gel electrophoresis. It was shown that acetylcholinesterase crosslinked in absence of Triton X-100 consists of molecular forms built up by dimeric protomers. These dimers were identical with the enzymatically active species sedimenting with 6.5S in linear sucrose density gradients.
mesh_terms: D000110:Acetylcholinesterase / Q000097:blood; D003432:Cross-Linking Reagents; D004119:Dimethyl Adipimidate; D004120:Dimethyl Suberimidate; D004910:Erythrocyte Membrane / Q000201:enzymology*; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D007096:Imidoesters; D046911:Macromolecular Substances; D008970:Molecular Weight; D013329:Structure-Activity Relationship
chemical_list: D003432:Cross-Linking Reagents; D007096:Imidoesters; D046911:Macromolecular Substances; D004119:Dimethyl Adipimidate; D004120:Dimethyl Suberimidate; D000110:Acetylcholinesterase