Open AccessPrimary structure of a low‐molecular‐mass N‐linked oligosaccharide from hemocyanin of Lymnaea stagnalis
Author(s) -
KUIK J. Albert,
SIJBESMA Rint P.,
KAMERLING Johannis P.,
VLIEGENTHART Johannes F. G.,
WOOD Edward J.
Publication year - 1986
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1986.tb10083.x
Subject(s) - lymnaea stagnalis , hemocyanin , fucose , molecular mass , biochemistry , chemistry , oligosaccharide , mannose , hemolymph , pyranose , glycan , glycosidic bond , snail , stereochemistry , glycoprotein , biology , ecology , genetics , antigen , enzyme
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 contaning 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‐NH 2 . Investigation with 500‐MHz 1 H‐NMR spectroscopy, in conjunction with sugar and methylation analysis revealed the lowest‐molecular‐mass glycan chain to have the structure: