Abstract
The keratan sulphate proteoglycans that can be prepared from bovine corneal stroma [Axelsson & Heinegård (1975) Biochem. J. 145, 491-500] were characterized by gel chromatography, gel electrophoresis and analytical ultracentrifugation in associative (0.6 M-NaCl) and dissociative (6M-guanidinum chloride) solvents. The proteoglycans aggreagated at low salt concentrations and pH. The weight-average molecular weight of the monomer proteoglycans was established. Keratan sulphate peptides and oligosaccharide peptides were isolated after proteolysis. Their composition indicated that both are linked to protein via asparagine residues. A tentative model for corneal keratan sulphate proteoglycans is suggested.