Interaction of concanavalin A with individual proteins from bacterial and mammalian ribosomes.

1.1. The interaction of 125I-labelled concanavalin A with individual proteins from Escherichia coli and rat liver ribosomes was analyzed.2.2. Ribosomal proteins were first separated by two-dimensional polyacrylamide gel electrophoresis. Gel slabs were then incubated with the radioactive lectin in the presence or absence of the competitor α-methyl-mannose, and the degree of specific binding was determined. Parallel experiments were carried out with known glycosylated and non-glycosylated reference proteins.3.3. It was mainly found that no significant interaction between ribosomal proteins and concanavalin A seems to occur.