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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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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.[1]

References

  1. Effects of common radioiodination procedures on the binding of glycoproteins to immobilized lectins. Montelaro, R.C., West, M., Ivey, M. Biochem. Biophys. Res. Commun. (1983) [Pubmed]
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