title: Ricinus communis agglutinin I reacting and non-reacting butyrylcholinesterase in human cerebrospinal fluid.
abstract: Differences in glycosylation of acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) 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 BuChE was almost fully bound to Con A, LCA and WGA-agarose. Brain BuChE was unable to react with RCA (RCA-BuChE), the plasma enzyme was completely bound to the lectin (RCA+BuChE) and BuChE from CSF of normal children was partially fixed to RCA (RCA +/- BuChE). BuChE in CSF of children with meningitis fully reacts with the lectin. The data suggest that the proportion of RCA+BuChE in CSF of children with meningitis is increased, this enzyme probably coming from plasma.
authors.affiliation: Departamento de Bioquímica y Biología Molecular A, Universidad de Murcia, Spain.
authors.forename: P L
authors.initials: PL
authors.lastname: Tornel
authors.forename: J
authors.initials: J
authors.lastname: Sáez-Valero
authors.forename: C J
authors.initials: CJ
authors.lastname: Vidal
mesh_terms: D000110:Acetylcholinesterase / Q000097:blood / Q000134:cerebrospinal fluid; D000373:Agglutinins / Q000494:pharmacology; D001921:Brain / Q000201:enzymology; D002091:Butyrylcholinesterase / Q000097:blood / Q000134:cerebrospinal fluid*; D006801:Humans; D037102:Lectins / Q000494:pharmacology*; D037121:Plant Lectins
chemical_list: D000373:Agglutinins; D037102:Lectins; D037121:Plant Lectins; C017707:Ricinus communis agglutinin-1; D000110:Acetylcholinesterase; D002091:Butyrylcholinesterase