A technique has been developed that utilizes affinity chromatography on Concanavalin A (Con A)-agarose column for isolation of glycopeptides from IgA protein. Three glycopeptides thus obtained were homogeneous when examined by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. One glycopeptide contained two oligosaccharides which were partially resolved following pronase digestion. Recovery of glycopeptides applied to the Con A column was virtually complete. The specificity of Con A for the glycopeptides present in the IgA1 protein was demonstrated. © 1976.