Abstract
We have investigated the relationship of concanavalin. A binding to the cell surface of normal and transformed cells and the subsequent agglutination of the transformed cells. At room temperature almost no differences could be detected in agglutinin binding between transformed and untransformed cells. At 0 degrees C, however, where endocytosis was negligible, the transformed cells bound three times more agglutinin. However, transformed cells and trypsin-treated normal cells do not agglutinate at 0 degrees C although the amounts of agglutinin bound at 0 degrees C are sufficient to permit agglutination when such cells are shifted up to room temperature. Both transformed and trypsin-treated normal cells show a marked increase in agglutination at 15 degrees C as compared to agglutination at 0 degrees C. From this, as well as the observation that mild glutaraldehyde fixation of the cell surface inhibited agglutination but not agglutinin binding, it was concluded that concanavalin A-mediated cell agglutination requires free movement of the agglutinin receptor sites within the plane of the cell surface.