Constitutional heterogeneity of the glycosaminoglycans in articular cartilage proteoglycans.
Proteoglycans were extracted from bovine articular cartilage with guanidine-HCl and fractionated in cesium chloride density gradients by equilibrium ultracentrifugation. The acidic glycosaminoglycan (AGAG) components were then determined enzymatically with chondroitinase-ABC and streptomyces hyaluronidase. Under associative and dissociative conditions, the distribution of the AGAG components was as follows: the ratio of 4-sulfated disaccharide units to total AGAG increased with decreasing density gradients whereas that of 6-sulfated disaccharide units to total AGAG increased with increasing density gradients. The ratio of disulfated disaccharide units to total AGAG increased somewhat with decreasing density gradients whereas that of non-sulfated disaccharide units tended to decrease. Although the cartilage proteoglycan macromolecules were heterogeneous, a certain regularity was observed with respect to the distribution of sulfate and the degree of sulfation in the chondroitin sulfate chains of the proteoglycans.
D000818:Animals; D002358:Cartilage, Articular / Q000032:analysis*; D002417:Cattle; D002809:Chondroitin Sulfates / Q000032:analysis; D004187:Disaccharides / Q000032:analysis; D005260:Female; D005690:Galactose / Q000032:analysis; D005965:Glucuronates / Q000032:analysis; D006595:Hexosamines / Q000032:analysis; D006820:Hyaluronic Acid / Q000032:analysis; D007632:Keratan Sulfate / Q000032:analysis; D011509:Proteoglycans / Q000032:analysis*
D004187:Disaccharides; D005965:Glucuronates; D006595:Hexosamines; D011509:Proteoglycans; D006820:Hyaluronic Acid; D002809:Chondroitin Sulfates; D007632:Keratan Sulfate; D005690:Galactose