The role of membrane bound glycoprotein on the permeability of liposomes.
The liposome permeability to potassium and methanosulfonate ions was determined in the presence of bound glycoprotein and protein. The permeability changes were registered by light-scattering measurements of the osmotic volume changes of liposome suspension after mixing with solutions containing K+ and MS- ions respectively. The permeability changes varied considerably with the change of glycoprotein-protein molar ratio in the liposomes. It was suggested that topological distribution of both molecules (glycoprotein and protein) in the lipid bilayer would play a substantial role and influence the permeability. It was confirmed from fluorescence measurements with ANS as a fluorescence marker. There was an increase of the number of binding sites (n) for ANS, increasing glycoprotein-protein molar ratio in the liposomes. These results were interpreted in terms of electrostatical changes of the membrane lipid region and membrane surface, caused by the interaction of glycoprotein and protein with lipids, as well as the associated role of these components on the permeability.
D000110:Acetylcholinesterase; D006023:Glycoproteins / Q000378:metabolism*; D008027:Light; D008081:Liposomes / Q000378:metabolism*; D008433:Mathematics; D008565:Membrane Proteins / Q000378:metabolism*; D009961:Orosomucoid; D010539:Permeability; D011485:Protein Binding; D012542:Scattering, Radiation; D013050:Spectrometry, Fluorescence
D006023:Glycoproteins; D008081:Liposomes; D008565:Membrane Proteins; D009961:Orosomucoid; D000110:Acetylcholinesterase