Primary structure of a low-molecular-mass N-linked oligosaccharide from hemocyanin of Lymnaea stagnalis. 3-O-methyl-D-mannose as a constituent of the xylose-containing core structure in an animal glycoprotein.
Hemocyanin from the freshwater snail Lymnaea stagnalis is a high-molecular-mass copper-containing oxygen-transport protein, which occurs freely dissolved in the hemolymph. It is a glycoprotein containing fucose, xylose, 3-O-methylmannose, 3-O-methylgalactose, mannose, galactose, N-acetylgalactosamine and N-acetylglucosamine residues as sugar constituents. The N-glycosidic carbohydrate chains of this glycoprotein were released by hydrazinolysis of a pronase digest and subsequently fractionated as oligosaccharide-alditols on Bio-Gel P-4 followed by Lichrosorb-NH2. Investigation with 500-MHz 1H-NMR spectroscopy, in conjunction with sugar and methylation analysis revealed the lowest-molecular-mass glycan chain to have the structure: (Formula: see text).
D000818:Animals; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D006023:Glycoproteins; D006433:Hemocyanins; D008195:Lymnaea; D008759:Methylglycosides / Q000032:analysis*; D008766:Methylmannosides / Q000032:analysis*; D009844:Oligosaccharides / Q000302:isolation & purification*; D011402:Pronase; D014994:Xylose / Q000032:analysis*
D006023:Glycoproteins; D008759:Methylglycosides; D008766:Methylmannosides; D009844:Oligosaccharides; C043123:3-O-methylmannose; D006433:Hemocyanins; D014994:Xylose; D011402:Pronase