GLYCOSYLATION OF CHOLINESTERASE FORMS IN BRAIN FROM NORMAL AND DYSTROPHIC LAMA2(DY) MICE

Differences in the oligosaccharides attached to acetyl- (AChE) and but yrylcholinesterase (BuChE) forms in brain from control and merosin-def icient Lama2(dy) dystrophic mice were investigated by means of their i nteraction with agarose-immobilized lectins. Asymmetric AChE, hydrophi lic 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) a nd Triticum vulgaris (WGA), and poorly so to Ricinus communis agglutin in (RCA), suggesting that the oligosaccharides in AChE or BuChE subuni ts are similarly processed regardless of their state of polymerization . The lack of differences in the interaction of lectins with homologou s AChE and BuChE forms in normal and dystrophic tissue indicates that, in contrast to ChEs forms in skeletal muscle, the dystrophic conditio n does not disturb the processing of the oligosaccarides of brain enzy me forms. (C) 1997 Elsevier Science Ireland Ltd.