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.
Okumura
Yukihisa
Y
Department of Chemistry and Material Engineering, Faculty of Engineering, Shinshu University, 4-17-1 Wakasato, Nagano 380-8553, Japan. okumura@shinshu-u.ac.jp
Mizushima
Hiroki
H
Sunamoto
Junzo
J
D000110:Acetylcholinesterase / Q000737:chemistry*; D000180:Acrylic Resins / Q000737:chemistry; D004134:Dimyristoylphosphatidylcholine / Q000737:chemistry*; D004800:Enzymes, Immobilized / Q000737:chemistry*; D004910:Erythrocyte Membrane / Q000737:chemistry; D005782:Gels; D017261:Glycosylphosphatidylinositols / Q000737:chemistry*; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D008081:Liposomes / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry
D000180:Acrylic Resins; D004800:Enzymes, Immobilized; D005782:Gels; D017261:Glycosylphosphatidylinositols; D008081:Liposomes; D008565:Membrane Proteins; C037239:Sephacryl Superfine; D000110:Acetylcholinesterase; D004134:Dimyristoylphosphatidylcholine