Relocation of active acetylcholinesterase to liposome–gel conjugate

Relocation of a glycosylphosphatidylinositol (GPI)-anchored protein acetylcholinesterase (AChE) in its enzymatically active form from proteovesicles containing human erythrocyte ghost membrane proteins onto a liposome–gel conjugate was examined. Liposomes of 1,2-dimyristoylphosphatidylcholine (DMPC) were immobilized on Sephacryl S-1000 gel that was chemically modified to bear hydrophobic octyl moieties. Upon coincubation of the liposome–gel conjugate with freely suspended proteovesicles prepared from erythrocyte ghosts, 50% of the AChE left the proteovesicles and immobilized onto the liposome–gel conjugate in 18 h. When the proteovesicles were immobilized and interacted with freely suspended plain liposomes, approximately 2% of the AChE appeared in the liposome fraction. The relocation of AChE apparently possesses strong preference for the liposome–gel conjugate, suggesting that the hydrophobic moieties on the gel could assist the relocation.

Relocation of a glycosylphosphatidylinositol-anchored protein, acetylcholinesterase (AChE), in its enzymatically active form from proteovesicles onto a liposome–gel conjugate was examined.Figure optionsDownload as PowerPoint slide