Effects of common radioiodination procedures on the binding of glycoproteins to immobilized lectins.
Representative glycoproteins including fetuin, protein A, ovalbumin, alpha 1 acid glycoprotein, and the major glycoprotein of equine infectious anemia virus were labelled with 125I by the chloramine-T or Bolton-Hunter procedure and their binding to immobilized Con A or lentil lectin compared to untreated samples of each glycoprotein. Glycoprotein modification was no greater than one substituted residue per protein molecule. Yet the radioiodinated glycoproteins typically displayed only 0-50% of the lectin binding observed with untreated samples. These results indicate that lectin glycoprotein binding can be markedly altered by minor modifications in protein structure.
D002846:Chromatography, Affinity / Q000379:methods; D006023:Glycoproteins / Q000302:isolation & purification; D007457:Iodine Radioisotopes; D007553:Isotope Labeling / Q000379:methods; D037102:Lectins; D013329:Structure-Activity Relationship
D006023:Glycoproteins; D007457:Iodine Radioisotopes; D037102:Lectins