Moya_1991_Comp.Biochem.Physiol.C_98_299

Reference

Title : A comparison of the Xenopus laevis oocyte acetylcholinesterase with the muscle and brain enzyme suggests variations at the post-translational level - Moya_1991_Comp.Biochem.Physiol.C_98_299
Author(s) : Moya MA , Fuentes ME , Inestrosa NC
Ref : Comparative Biochemistry & Physiology C Pharmacol Toxicol , 98 :299 , 1991
Abstract :

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.

PubMedSearch : Moya_1991_Comp.Biochem.Physiol.C_98_299
PubMedID: 1676945

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Citations formats

Moya MA, Fuentes ME, Inestrosa NC (1991)
A comparison of the Xenopus laevis oocyte acetylcholinesterase with the muscle and brain enzyme suggests variations at the post-translational level
Comparative Biochemistry & Physiology C Pharmacol Toxicol 98 :299

Moya MA, Fuentes ME, Inestrosa NC (1991)
Comparative Biochemistry & Physiology C Pharmacol Toxicol 98 :299