A COMPARISON OF THE XENOPUS-LAEVIS OOCYTE ACETYLCHOLINESTERASE WITH THE MUSCLE AND BRAIN ENZYME SUGGESTS VARIATIONS AT THE POSTTRANSLATIONAL LEVEL
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1991
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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.
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.