Acetylcholinesterases from Musca domestica and Drosophila melanogaster Brain Are Linked to Membranes by a Glycophospholipid Anchor Sensitive to an Endogenous Phospholipase
- 1 April 1988
- journal article
- research article
- Published by Wiley in Journal of Neurochemistry
- Vol. 50 (4) , 1158-1163
- https://doi.org/10.1111/j.1471-4159.1988.tb10587.x
Abstract
The sensitivity of acetylcholinesterases (AChEs) from Musca domestica and from Drosophila melanogaster to the phosphatidylinositol‐specific phospholipase C from Bacillus cereus and to the glycosylphosphatidylinositol‐specific phospholipase C from Trypanosoma brucei was investigated. B. cereus phospholipase C solubilizes membrane‐bound AChE, and both phospholipases convert amphiphilic AChEs into hydrophilic forms of the enzyme. The Upases uncover an immunological determinant that is found on other glycosylphosphatidylinositol‐anchored membrane proteins after the same treatment. This immunological determinant is also present on the native hydrophilic form of AChE. The polypeptide bearing the active site of the membrane‐bound enzyme migrates faster during sodium dodecyl sulfate‐polyacrylamide gel electrophoresis than the same polypeptide from the soluble enzyme. We conclude that AChE from insect brain is attached to membranes via a glycophospholipid anchor. This anchor is covalently linked to the polypeptide bearing the active esterase site of the enzyme and can be cleaved by an endogenous lipase.Keywords
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