Heterogeneity, polydispersity, and physiologic role of corneal proteoglycans.
Gel chromatography, affinity chromatography, ultracentrifugation, enzymic fragmentation, and analysis of amino acids, hexosamines and neutral sugars were used to characterize a heterogeneous fraction of proteoglycans from bovine corneal stroma. The results indicate that the fraction largely consists of a mixture of the 2 main types of corneal proteoglycans described earlier, namely keratan sulfate proteoglycans and chondroitin sulfate-rich proteoglycans with covalently bound oligosaccharides. Models for the structure of proteoglycans are suggested, an it is concluded that the molecular size of corneal proteoglycans makes them appropriate as 'spacers' between the collagen fibrils, a property important for corneal transparency. Cornea is softer than cartilage because corneal proteoglycans are less underhydrated than cartilage proteoglycans.
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002499:Centrifugation, Density Gradient; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D003315:Cornea / Q000032:analysis*; D003319:Corneal Stroma / Q000032:analysis*; D008297:Male; D011509:Proteoglycans / Q000032:analysis* / Q000502:physiology; D051381:Rats; D011919:Rats, Inbred Strains; D014802:Vitamin A Deficiency / Q000378:metabolism
D011509:Proteoglycans