Partial isolation and characterization of Gp 220, the Ulex europaeus binding glycoprotein of the B-lymphocyte plasma membrane.
Using affinity chromatography on Sepharose 4B coupled with Ulex europaeus lectin, a partially purified gp 220 was isolated from the RAJI cell membrane. This protein could not be isolated from the membranes of the T-cell line MOLT-4 nor from human erythrocytes. Gp 220 is composed of three subunits gp 85, 70 and 65 held together by disulfide bridges. Gp 85 contains fucosyl residues, gp 70 contains galactosyl residues, and gp 65 contains both sugars. Gp 220 is different from fibronectin and spectrin, proteins which also show binding to the Ulex europaeus lectin.
D000596:Amino Acids; D001402:B-Lymphocytes / Q000276:immunology*; D001665:Binding Sites; D002462:Cell Membrane / Q000276:immunology; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D005353:Fibronectins; D006023:Glycoproteins / Q000302:isolation & purification*; D006801:Humans; D037102:Lectins / Q000302:isolation & purification*; D008970:Molecular Weight; D013049:Spectrin
D000596:Amino Acids; D005353:Fibronectins; D006023:Glycoproteins; D037102:Lectins; D013049:Spectrin