Partial characterization of the heteropolysaccharide associated with the 7S domain of type IV collagen from placenta.
A major heteropolysaccharide fraction was isolated from the 7S domain of human placental type IV collagen. Analyses revealed that it was an asparagine-linked oligosaccharide. Characterization using molecular sieve chromatography, exoglycosidase and endoglycosidase digestion, and chemical analysis suggested a bianternnary complex with the following structure: (Formula: see text) A microheterogeneity was noted with respect to the addition of the fucose and sialic acid residues. Analysis of component polypeptides of the 7S fraction following endoglycosidase treatment suggested that the most obvious site of heteropolysaccharide attachment was in a polypeptide of relative mass 40,000. Amino acid analysis of this isolated polypeptide indicated that it was rich in collagenous sequences and also contained half-cystine residues.
D000596:Amino Acids / Q000032:analysis; D001894:Borohydrides; D002241:Carbohydrates / Q000032:analysis; D003094:Collagen / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006801:Humans; D066298:In Vitro Techniques; D008970:Molecular Weight; D010455:Peptides / Q000032:analysis; D010920:Placenta / Q000032:analysis*; D011134:Polysaccharides / Q000032:analysis*; D011247:Pregnancy; D011489:Protein Denaturation
D000596:Amino Acids; D001894:Borohydrides; D002241:Carbohydrates; D010455:Peptides; D011134:Polysaccharides; C025364:sodium borohydride; D003094:Collagen