Glycopeptides isolated by exhaustive pronase digestion from the egg jelly coat of toad, Bufo vulgaris, were separated by DEAE-cellulose chromatography into two fractions. These fractions each gave a single band when they were subjected to electrophoresis on cellulose acetate strips. The glycopeptides behaved as a kind of "macroglycopeptide" on gel chromatography. 2. The glycopeptide fractions contained as sugar components galactosamine, glucosamine, galactose, fucose and N-acetylneuraminic acid. The amino acid composition was characterized by the presence of threonine and serine, which accounted for approximately 70% of the total amino acids. 3. Large amounts of galactosamine, threonine and serine were destroyed by treatment with alkali, indicating that the carbohydrate-peptide linkage in the glycopeptides is mostly an O-glycosidic bond between N-acetylgalactosamine and the hydroxy groups of threonine and serine.