Recognition of monosialoganglioside (GM3) reconstituted in sphingomyerin and glucosylceramide membranes against wheat germ agglutinin: quantitative analyses by a quartz crystal microbalance.
Specific binding of Wheat Germ Agglutinin (WGA) to GM3-containing mixed monolayer at the air-water interface was studied by using a quartz crystal microbalance to know the binding amount and initial binding rate of WGA to GM3. GM3 in the glucosylceramide matrix membrane showed the high recognizability compared to GM3 in sphingomyeline matrix membrane. It is demonstrated that matrix lipids surrounding GM3 regulated the recognition of GM3.
Sato
T
T
Department of Biomolecular Engineering, Tokyo Institute of Technology, Yokohama, Japan.
Serizawa
T
T
Okahata
Y
Y
D001665:Binding Sites; D005679:G(M3) Ganglioside / Q000378:metabolism*; D005963:Glucosylceramides / Q000378:metabolism*; D007700:Kinetics; D008567:Membranes, Artificial; D011791:Quartz; D013109:Sphingomyelins / Q000378:metabolism*; D014909:Wheat Germ Agglutinins / Q000378:metabolism*
D005679:G(M3) Ganglioside; D005963:Glucosylceramides; D008567:Membranes, Artificial; D013109:Sphingomyelins; D014909:Wheat Germ Agglutinins; D011791:Quartz