A comparison of the Xenopus laevis oocyte acetylcholinesterase with the muscle and brain enzyme suggests variations at the post-translational level.
1. Xenopus laevis oocytes express endogenously two components of the cholinergic system: the muscarinic receptors and the acetylcholinesterase (AChE). 2. A biochemical characterization of this enzyme was carried out. 3. The results established that the activity found in the oocytes correspond to 'true' AChE with a molecular weight of 65,000 Da and a sedimentation coefficient of 3-4 S. 4. The enzyme aggregates in the absence of detergent suggesting that it possess an hydrophobic character; despite that, it is not sensitive to PIPLC. 5. A comparison with the Xenopus brain and muscle AChE shows different post-translational modifications and catalytic properties with the oocyte AChE.
Department of Cell and Molecular Biology, Faculty of Biological Sciences, Catholic University of Chile, Santiago.
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Moya
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Fuentes
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Inestrosa
D000110:Acetylcholinesterase / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D001921:Brain / Q000201:enzymology*; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002800:Cholinesterase Inhibitors / Q000494:pharmacology; D002846:Chromatography, Affinity / Q000379:methods; D005260:Female; D007700:Kinetics; D037102:Lectins / Q000378:metabolism; D009132:Muscles / Q000201:enzymology*; D009865:Oocytes / Q000201:enzymology*; D011499:Protein Processing, Post-Translational / Q000502:physiology*; D013696:Temperature; D014982:Xenopus laevis
D002800:Cholinesterase Inhibitors; D037102:Lectins; D000110:Acetylcholinesterase