The properties of a complex of the mucopolysaccharide and proteins of the cornea

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Abstract
The tyrosine, tryptophan and hydroxyproline contents and the reaction with collagenase indicate that corneal mucoid contains proteins which are not collagen derivatives. The mucoid migrates with a single boundary on electrophoresis in the range pH 2-11.5. At higher pH, or in presence of guanidine, the peak is asymmetric and the mucoid behaves as an equilibrium mixture with its dissociation products. Osmotic pressure measurements reveal that the mucoid is dissociated by urea or at pH 12. These effects are partly reversible. The derived mucopolysaccharide sediments with a single boundary in the ultracentrifuge. The mucoid has 3 components in salt solutions, but in urea solution it moves with a single boundary. A mixture of the mucoid and mucopolysaccharide in urea solution sediments with a single boundary. The relevance of these observations to the problem of the protein-mucopoly-saccharide linkage is discussed and the hypothesis put forward that it is due to ion-pair formation between sulfuric ester groups and the amidine groups of arginine residues.