Collagen preparations from bovine tissues were analysed for their carbohydrate content. Crude preparations of tropocollagen and polymeric collagen were found to be contaminated with considerable amounts of mannose, fucose and hexosamine, sugars known to be present in the mucoprotein of the interfibrillar material with which collagen is associated in vivo. A pure preparation of tropocollagen obtained by ethanol precipitation procedures contained only galactose and glucose in the approximate ratio of 7:3 residues/3000 amino acid residues. Purification of crude polymeric collagen by EDTA extraction or by crude bacterial amylase extraction considerably decreased the mucoprotein contamination, particularly in the enzymic treatment, which yielded a preparation containing predominantly galactose and glucose in the ratio of 4:2 residues/3000 amino acid residues. The results confirm previous work that demonstrated the purity of these collagen preparations as inferred by amino acid analysis. The results also indicate the suitability of the pure tropocollagen and the amylase-extracted polymeric collagen for studies on the role of the carbohydrate residues in intramolecular and intermolecular cross-linking in collagen.