Abstract
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.
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