Séparation et purification des sites récepteurs de la lectine de Robinia et de la concanavaline a, présents à la surface des cellules hépatiques normales et tumorales (hépatome de zajdéla)

Abstract

This report describes separation and purification of cell-surface components possessing Robinia lectin and concavanalin A activities from rat normal liver and ascites hepatoma cells. Limited treatment of both normal and transformed cells with trypsin releases a glycopeptide fraction from the cell surface. These fractions inhibit agglutinaton and (or) growth inhibition of Robinia lectin and concanavalin A, indicating that receptor sites for both lectins are components of the cell surface glycopeptide fraction. The successive stages of purification of binding sites were followed by measuring the ability of the various fractions to inhibit the cell agglutination and cell growth with the corresponding lectins. The cell surface glycopeptide fraction was fractionated by repeated gel filtraton into fractions, two of which are more than 50 times as effective as the trypsin proteolysate. The differences in biological activities displayed by the cell surface lectin receptors from normal and transformed cells support the belief that these two types of binding sites are different.