TY - JOUR
T1 - Interactions of plant lectins with glycolipids in liposomes
AU - Boldt, David H.
AU - Speckart, Stephen F.
AU - Richards, Roberta L.
AU - Alving, Carl R.
PY - 1977/1/10
Y1 - 1977/1/10
N2 - A panel of five plant lectins with different binding specificities was used to determine if plant lectins could bind specifically to membrane-associated glycolipids. Ricinis communis and wheat germ agglutinins both bound specifically to mixed brain gangliosides and globoside I from human erythrocytes. Wheat germ agglutinin also bound to ganglioside GM1 and human erythrocyte ceramide trihexoside, but not to ceramide dihexoside, mono-, or digalactosyl diglycerides. Concanavalin A bound to liposomes with or without glycolipid substituents, and this binding was partially inhibited by α-methyl mannoside. This study indicates that lectins can specifically recognize and bind to certain glycolipids in membranes.
AB - A panel of five plant lectins with different binding specificities was used to determine if plant lectins could bind specifically to membrane-associated glycolipids. Ricinis communis and wheat germ agglutinins both bound specifically to mixed brain gangliosides and globoside I from human erythrocytes. Wheat germ agglutinin also bound to ganglioside GM1 and human erythrocyte ceramide trihexoside, but not to ceramide dihexoside, mono-, or digalactosyl diglycerides. Concanavalin A bound to liposomes with or without glycolipid substituents, and this binding was partially inhibited by α-methyl mannoside. This study indicates that lectins can specifically recognize and bind to certain glycolipids in membranes.
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U2 - 10.1016/0006-291X(77)91395-X
DO - 10.1016/0006-291X(77)91395-X
M3 - Article
C2 - 836279
AN - SCOPUS:0017597888
VL - 74
SP - 208
EP - 214
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 1
ER -