Abstract
Differences in the oligosaccharides attached to acetyl- (AChE) and butyrylcholinesterase (BuChE) forms in brain from control and merosin-deficient Lama2 dy 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.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
