Effect of ConA-receptor interaction on the structure of cell membrane

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Recently,the effect of ligand receptor interaction onthe membrane structure of liposomes has been studied ex-tensively.However,little is known about how it exists onbiological membranes.In this paper,the effect of Con-canavalin A(ConA)receptor interaction on the structure ofcell membranes was studied by Circular Dichroism(CD)and31P Nuclear Magnetic Resonance(NMR). CD results of both the purified macrophage membranesand human erythrocyte ghosts(EG)showed that the con-formation of membrane proteins changed after ConA bind-ing. For further research,31P-NMR was used to detect theorganization of phospholipid molecules on macrophage mem-branes.After ConA binding,the tendency to form non bi-layer structure increased with the amount of ConA.Thechanges of 31P-NMR spectra of living macrophages mightbe partly due to the above stated reason too. In addition,ConA-receptor interaction also inducedsimilar results of 3lP-NMR spectra in EG.In contrast,wheat germ agglutinin(WGA),another kind of lectin,rarely showed the same influence. Recently, the effect of ligand receptor interaction on the membrane structure of liposomes has been studied ex-tensively. However, little is known about how it has onbiological membranes. In this paper, the effect of Con-canavalin A (Con A) receptor interaction on the structure of cell membranes was studied by Circular Dichroism (CD) and 31P Nuclear Magnetic Resonance (NMR). CD results of both the purified macrophage membranes and human erythrocyte ghosts (EG) showed that the con-formation of membrane proteins changed after ConA bind-ing. For Further research, 31P-NMR was used to detect the organization of phospholipid molecules on macrophage mem-branes. After ConA binding, the tendency to form non bi-layer structure increased with the amount of ConA. Thechanges of 31P-NMR spectra of living macrophages mightbe partly due to the above stated reason too. In addition, ConA-receptor interaction also induced similar results of 3lP-NMR spectra in EG. contrast, wheat germ agglutinin (WGA), another kind of lect in, rarely showed the same influence.
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