Tornel_1992_Neurosci.Lett_145_59

Differences in glycosylation of acetylcholinesterase (AChE) and butyrylcholinesterase (BCHE) in human brain, plasma and cerebrospinal fluid (CSF) have been investigated by means of their interaction with agarose-immobilized lectins. Most of the AChE in brain and CSF was associated to concanavalin A (Con A), Lens culinaris (LCA) and Triticum vulgaris (WGA) agglutinins, but little activity was adsorbed to Ricinus communis agglutinin I (RCAI). Brain, plasma and CSF BCHE was almost fully bound to Con A, LCA and WGA-agarose. Brain BCHE was unable to react with RCA (RCA-BCHE), the plasma enzyme was completely bound to the lectin (RCA+BCHE) and BCHE from CSF of normal children was partially fixed to RCA (RCA +/- BCHE). BCHE in CSF of children with meningitis fully reacts with the lectin. The data suggest that the proportion of RCA+BCHE in CSF of children with meningitis is increased, this enzyme probably coming from plasma.