Cabezas-Herrera_1994_Biochim.Biophys.Acta_1225_283

Differences in glycosylation between molecular forms of acetylcholinesterase (AChE) and butyrylcholinesterase (BCHE) in muscle and serum of normal and dystrophic mice have been studied by means of their adsorption to immobilized lectins. Application of a two-step extraction procedure, first with saline buffer, and second with saline buffer and Triton X-100, brought into solution most of the muscle AChE and BCHE activities. The AChE activity was five times greater than that of BCHE in normal (NM) and dystrophic muscle (DM). The AChE activity in the serum of dystrophic mice was twice that measured in control animals, but the BCHE activity remained almost unchanged. Both AChE and BCHE in muscle and serum bound completely to concanavalin A (Con A) and Lens culinaris agglutinin (LCA). A12, A8 and G4 AChE, but not the light G2 and G1 AChE forms, in NM and DM were completely adsorbed to wheat germ agglutinin (WGA). Similarly, G4 BCHE, but not the G2 and G1 forms, were associated to WGA. A high proportion of G4 and G1 AChE and G4 BCHE forms in mouse serum were fixed to WGA. Asymmetric AChE in NM and DM reacted with Ricinus communis agglutinin (RCA) but the light AChE and BCHE forms in muscle and serum did not bind to the lectin. G4 AChE and G4 BCHE in NM were not recognized by RCA, but the isoforms in DM bound fully to the lectin. Serum G4 AChE from control or dystrophic mice did not react with RCA, but G4 BCHE was fixed to the lectin. Since RCA is specific for galactose, the results suggest that in dystrophic muscle galactose is incorporated early in G4 AChE and this affects the level of the functional tetramers destined for insertion in the plasma membrane.