Influence of temperature on the interaction of Concanavalin A with chick fibroblasts during embryo development

Abstract

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°, 21° and 37°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.