INFLUENCE OF TEMPERATURE ON THE INTERACTION OF CONCANAVALIN A WITH CHICK FIBROBLASTS DURING EMBRYO DEVELOPMENT

The interaction between concanavalin A and chick embryo fibroblasts was studied. Cells from younger and older embryos had the same number of lectin receptor sites per cell at 4.degree., 21.degree. and 37.degree. C, but the affinity constants increased with increasing temperature. Analysis of the binding data according to Scatchard showed that the apparent changes in binding as a function of temperature might be related to thermodynamic properties. The lectin binding sites on the cell surface proved homogeneous with regard to binding properties. The age-related differences noted in the affinities of the cells to bind concanavalin A could be related to differences in the degree of rearrangement of the cell surface components and/or to a change in the structure of cell surface glycoconjugates, and may serve to explain the differences in the effect of concanavalin A on cell growth.