title: Evidence for the presence of a mammalian-like cholinesterase in Paramecium primaurelia (Protista, Ciliophora) developmental cycle.
abstract: By histochemical and immunohistochemical methods, the presence of cholinergic-like molecules has previously been demonstrated in Paramecium primaurelia, and their functional role in mating-cell pairing was suggested. In this work, both true acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) activities were electrophoretically investigated, and the presence of molecules immunologically related to BuChE was checked by immunoblotting. The AChE activity, shown in the membrane protein fraction of mating-competent cells and in the cytoplasmic fraction of immature cells, is due to a 260-kDa molecular form, similar to the membrane-bound tetrameric form present in human erythrocytes. This AChE activity does not appear in either the cytoplasmic fraction of mating-competent cells or in the membrane protein fraction of immature cells. No evidence was found for the presence or the activity of BuChE-like molecules. The role of AChE in P. primaurelia developmental cycle is discussed.
authors.affiliation: Institute of Zoology, University of Genoa, Italy. zoologia@cisi.igecuniv.unige.it
authors.forename: M U
authors.initials: MU
authors.lastname: Delmonte Corrado
authors.forename: H
authors.initials: H
authors.lastname: Politi
authors.forename: F
authors.initials: F
authors.lastname: Trielli
authors.forename: C
authors.initials: C
authors.lastname: Angelini
authors.forename: C
authors.initials: C
authors.lastname: Falugi
mesh_terms: D000110:Acetylcholinesterase / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D002091:Butyrylcholinesterase / Q000302:isolation & purification / Q000378:metabolism*; D008565:Membrane Proteins / Q000737:chemistry; D010247:Paramecium / Q000201:enzymology*; D012098:Reproduction