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.