Evidence for the presence and structure of asparagine-linked oligosaccharide units in the core protein of proteodermatan sulphate.
The N-glycosidically linked oligosaccharides were liberated by hydrazinolysis from purified proteodermatan sulphate from newborn-calf skin and reduced with NaB3H4 at the reducing terminal sugar. One asparagine-linked oligosaccharide chain was linked to one core-protein molecule in proteodermatan sulphate. Structural sequences were analysed by using exoglycosidase digestion. These oligosaccharides were composed of di- and tri-antennary oligosaccharide structures of complex type.
D000818:Animals; D001216:Asparagine / Q000032:analysis; D001894:Borohydrides; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D002807:Chondroitin / Q000031:analogs & derivatives*; D002850:Chromatography, Gel; D003871:Dermatan Sulfate / Q000031:analogs & derivatives*; D004590:Electrophoresis, Paper; D006026:Glycoside Hydrolases; D006834:Hydrazines; D009844:Oligosaccharides / Q000032:analysis*; D011509:Proteoglycans; D012794:Sialic Acids / Q000032:analysis
D001894:Borohydrides; D006834:Hydrazines; D009844:Oligosaccharides; D011509:Proteoglycans; D012794:Sialic Acids; C028774:proteodermatan sulfate; D003871:Dermatan Sulfate; C029424:hydrazine; D001216:Asparagine; C025364:sodium borohydride; D002807:Chondroitin; D006026:Glycoside Hydrolases