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. 