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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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.

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