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Phosphoglycans from the cell wall of many strains of Streptococci contain terminal carbohydrate units linked by phosphodiester bridges to other residues of the glycans. In the immune response to phosphoglycans, the terminal carbohydrate-phosphate moieties function as antigenic determinants and induce the synthesis of antibodies with specificity for the glycosyl-phosphoryl units. It has now been found that such terminal carbohydrate units can be removed by treatment of the glycans with appropriate glycosidases. Thus, an almond beta-glucosidase releases glucose from a streptococcal Group D phosphoglycan with beta-glucosyl phosphate units, a jack bean N-acetyl-beta-glucosaminidase releases N-acetylglucosamine from a streptococcal Group L phosphoglycan with N-acetyl-beta-glucosaminyl phosphate units, and a rice alpha-glucosidase releases glucose from a yeast phosphoglycan with alpha-glucosyl phosphate units. The glycosidases also hydrolyze the hexose phosphates of the proper anomeric configuration and structure. The preparations of glycosidases used in this study exhibit specificity for single types of carbohydrate residues and are devoid of phosphatase and phosphodiesterase activities. The glycosidases act on glycosyl-phosphoryl linkages by a stereospecific mechanism and can therefore be used for the determination of the anomeric configuration of glycosyl-phosphoryl units of complex carbohydrates.

The glucose-containing, membrane-derived oligosaccharides of Escherichia coli are localized in the external envelope of that organism, most probably in the periplasmic space. The membrane-derived oligosaccharides appear to be generally occurring cell constituents of gram-negative (but not gram-positive) bacteria.