Heterogeneity of the carbohydrate chains of sulfated bronchial glycoproteins isolated from a patient suffering from cystic fibrosis.

Sulfated glycoproteins having blood group H activity were isolated from the sputum of a child suffering from cystic fibrosis, by reduction of the fibrillar mucus, chromatography on ECTEOLA-cellulose, and gel filtration on Sepharose 4B. The sulfated glycoproteins were degraded with alkaline borohydride, and the degradation products were fractionated by chromatography on ion exchange resins and by gel filtration. The carbohydrate chains thus obtained have a wide heterogeneity with regard to acidity and molecular size. The neutral chains contain blood group H active oligosaccharides and incomplete chains as short as 1 residue of 2-acetamido-2-deoxy-D-galactose. The minimal size of the neuraminic acid-containing chains is less than that of the sulfated chains, which increases with the degree of sulfation. The sulfate groups are linked at C-6 at the D-galactose residues.