XB-ART-25323
Comp Biochem Physiol C Comp Pharmacol Toxicol
1991 Jan 01;982-3:299-305. doi: 10.1016/0742-8413(91)90209-c.
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A comparison of the Xenopus laevis oocyte acetylcholinesterase with the muscle and brain enzyme suggests variations at the post-translational level.
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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.
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Species referenced: Xenopus laevis
Genes referenced: ache