Squid proteoglycans: isolation and characterization of three populations from cranial cartilage.
Squid cranial cartilage is poor in proteoglycans. They were extracted by 2% SDS and purified by isopycnic centrifugation in the presence of detergent. According to their buoyant density and hydrodynamic size they were fractionated into three structurally different populations of Mr 1.3.10(6), 0.6.10(6) and 1.0.10(6). The proteoglycans of each population differ in the number of oversulphated chondroitin sulphate chains, ranging from two to five, in the number and size of uronic acid and sulphate containing oligosaccharides and in the size of their core protein. The majority, if not all, of the oligosaccharides are linked to the protein via an O-glycosidic bond involving galactosamine and most likely xylose. The chondroitin sulphate chains are segregated on a small peptide segment of the molecule which also contains a large proportion of the oligosaccharides. The proteoglycans have no tendency to interact with hyaluronate.
Vynios
D H
DH
Department of Chemistry, University of Patras, Greece.
Tsiganos
C P
CP
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002356:Cartilage / Q000378:metabolism*; D002809:Chondroitin Sulfates / Q000032:analysis; D002850:Chromatography, Gel; D049832:Decapodiformes; D009844:Oligosaccharides / Q000032:analysis; D011509:Proteoglycans / Q000032:analysis / Q000302:isolation & purification*; D012886:Skull; D014357:Trypsin
D000596:Amino Acids; D009844:Oligosaccharides; D011509:Proteoglycans; D002809:Chondroitin Sulfates; D014357:Trypsin