Structural studies on a sulphated glycoprotein preparation isolated from human saliva.
The identity of the sulphated component in a high-molecular-weight glycoprotein preparation (GP) from human whole saliva was investigated. A t0.5 of 96 min for inorganic sulphate release in 0.25 M HCl indicated the presence of O-substituted sulphate, probably associated with hydroxyl groups of sugar residues. This possible association of ester was also inferred from infra-red data of the intact GP, where major absorption bands were detected at 1230-1250 and 828 cm-1. Further a sulphated-monosaccharide derivative was released during acid hydrolysis in 0.1 M HCl at 100 degrees C for 75 min and isolated by gel-filtration on Sephadex G-15. This derivative was separated from a range of non-sulphated sugars by thin-layer chromatography in various solvent systems and possessed the chromatographic characteristics of N-acetylgalactosamine-6-O-sulphate.
D000116:Acetylgalactosamine / Q000031:analogs & derivatives; D002855:Chromatography, Thin Layer; D051152:Clusterin; D006023:Glycoproteins / Q000032:analysis*; D006801:Humans; D006868:Hydrolysis; D018832:Molecular Chaperones; D008970:Molecular Weight; D012471:Salivary Proteins and Peptides / Q000032:analysis*
C495242:CLU protein, human; D051152:Clusterin; D006023:Glycoproteins; D018832:Molecular Chaperones; D012471:Salivary Proteins and Peptides; C046735:N-acetylgalactosamine 4-sulfate; D000116:Acetylgalactosamine