Glycosylation of cholinesterase forms in brain from normal and dystrophic Lama2dy mice.

Differences in the oligosaccharides attached to acetyl- (AChE) and butyrylcholinesterase (BuChE) forms in brain from control and merosin-deficient Lama2dy dystrophic mice were investigated by means of their interaction with agarose-immobilized lectins. Asymmetric AChE, hydrophilic and amphiphilic AChE and BuChE tetramers, and amphiphilic AChE and BuChE monomers were identified in brain. All ChE forms were strongly adsorbed to the lectins concanavalin A (Con A), Lens culinaris (LCA) and Triticum vulgaris (WGA), and poorly so to Ricinus communis agglutinin (RCA), suggesting that the oligosaccharides in AChE or BuChE subunits are similarly processed regardless of their state of polymerization. The lack of differences in the interaction of lectins with homologous AChE and BuChE forms in normal and dystrophic tissue indicates that, in contrast to ChEs forms in skeletal muscle, the dystrophic condition does not disturb the processing of the oligosaccarides of brain enzyme forms.