Montelaro R C, West M, Ivey M
Biochem Biophys Res Commun. 1983 Jan 14;110(1):103-7. doi: 10.1016/0006-291x(83)91266-4.
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.
包括胎球蛋白、蛋白A、卵清蛋白、α1酸性糖蛋白以及马传染性贫血病毒主要糖蛋白在内的代表性糖蛋白，通过氯胺-T法或博尔顿-亨特法用125I进行标记，并将它们与每种糖蛋白的未处理样品相比，观察其与固定化伴刀豆球蛋白A或扁豆凝集素的结合情况。糖蛋白修饰程度不超过每个蛋白质分子一个取代残基。然而，放射性碘化糖蛋白与未处理样品相比，通常仅显示出0-50%的凝集素结合。这些结果表明，蛋白质结构的微小修饰可显著改变凝集素与糖蛋白的结合。
