Analysis of glycoproteins from nasal polyps and papillomas by affinity chromatography.

Abstract

Glycoproteins were isolated from the particulate fraction of four nasal polyps and three nasal papillomas by affinity chromatography on lectins conjugated with agarose (Concanavalin A [Con A], wheat germ agglutinin [WGA], Ricinus communis agglutinin [RCA], peanut agglutinin [PNA], and Dolichos biflorus agglutinin [DBA]). The glycoprotein mixtures so isolated were then analyzed by sodium dodecyl sulfate gel electrophoresis. Glycoprotein profiles of nasal polyps were similar to each other, but were distinctively different from those of nasal papillomas. Binding sites for Con A, WGA, and RCA isolated from nasal papillomas contained intense bands with a molecular weight less than 15,000 daltons, which were absent in nasal polyps. The major component of PNA-binding sites of nasal polyps is of a molecular weight of 65,000 daltons, which was not detected in nasal papillomas.