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Primary structure of the low-molecular-weight carbohydrate chains of Helix pomatia alpha-hemocyanin. Xylose as a constituent of N-linked oligosaccharides in an animal glycoprotein.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 1985 Nov 15; Vol. 260 (26), pp. 13984-8. - Publication Year :
- 1985
-
Abstract
- alpha-Hemocyanin of Helix pomatia is a copper-containing glycoprotein which serves as an oxygen carrier in the hemolymph. Its carbohydrate moiety has as constituents fucose, xylose, 3-O-methylgalactose, mannose, galactose, N-acetylgalactosamine, and N-acetyl-glucosamine residues. Alkaline borhydride did not split off any carbohydrate material, suggesting the absence of O-glycosidic chains. The N-glycosidic carbohydrate chains of this glycoprotein were liberated by hydrazinolysis of a Pronase digest then fractionated as alditols on Bio-Gel P-4. The fractions containing the low-molecular-weight glycans were investigated by 500-MHz 1H NMR spectroscopy in conjunction with sugar and methylation analysis. The largest, and most abundant, compound was established to be: (Formula: see text). Another compound was characterized as the afuco analogue of this structure. H. pomatia alpha-hemocyanin is the first example of an animal glycoprotein having xylose as a constituent of N-glycosidic carbohydrate chains.
- Subjects :
- Acetylglucosamine analysis
Animals
Borohydrides pharmacology
Carbohydrate Conformation
Carbohydrate Sequence
Carbohydrates analysis
Fucose analysis
Magnetic Resonance Spectroscopy
Mannose analysis
Molecular Weight
Pronase metabolism
Helix, Snails analysis
Hemocyanins analysis
Oligosaccharides analysis
Xylose analysis
Subjects
Details
- Language :
- English
- ISSN :
- 0021-9258
- Volume :
- 260
- Issue :
- 26
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 4055767