The role of interfacial structured water on the glycoprotein arrangement in liposomes.
The effect of perturbing the interfacial water structure in liposomes on the glycoprotein arrangement in the bilayer was investigated. This perturbation was achieved by a series of reagents called structure makers and breakers. The glycoprotein arrangement in the liposomes was determined by fluorescence measurement with 1-anilino-2-naphthalene sulphonate (ANS). A dependence of (n) (number of binding sites for ANS on the glycoprotein molecule) with concentration of structure maker and breaker reagents was observed. The results have been interpreted as a possible new arrangement of membrane-bound glycoprotein, due to the effect of perturbing the interfacial water structure in the liposomes.
D000817:Anilino Naphthalenesulfonates; D002784:Cholesterol; D006023:Glycoproteins; D008051:Lipid Bilayers; D008081:Liposomes; D008565:Membrane Proteins; D008744:Methylamines; D010059:Ovomucin; D010713:Phosphatidylcholines; D013050:Spectrometry, Fluorescence; D014508:Urea; D014867:Water
D000817:Anilino Naphthalenesulfonates; D006023:Glycoproteins; D008051:Lipid Bilayers; D008081:Liposomes; D008565:Membrane Proteins; D008744:Methylamines; D010713:Phosphatidylcholines; D014867:Water; D010059:Ovomucin; D014508:Urea; D002784:Cholesterol