Abstract
A C-type lectin (BRA-2) isolated from the acorn barnacle Megabalanus rosa, which was a glycoprotein having an N-linked sugar chain, was deglycosylated by N-glycopeptidase F. The structure of the released sugar chains was determined by a 2-D mapping method after derivatization with a fluorescent reagent, 2-aminopyridine, to be Manα1-6(Manα1-3)Manβ1-4GlcNAcβ1- 4(Fucα1-6)GlcNAc and Manα1-6(GlcNAcβ1-2Manα1-3) Manβ1-4GlcNAcβ1-4(Fucα1-6)GlcNAc. The structures were confirmed by matrix-assisted laser desorption ionization mass spectrometry and a comparison with authentic sugar chains by high-pressure liquid chromatography. Various properties of BRA-2 were examined before and after deglycosylation. The susceptibility of BRA-2 to protease digestion was increased by deglycosylation. However, the inhibitory activity toward calcium carbonate crystallization as well as the hemagglutinating activity of deglycosylated BRA-2 was significantly decreased. These results suggest that the sugar chains of BRA-2 are important to both its structural stability and its function.
Original language | English |
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Pages (from-to) | 931-940 |
Number of pages | 10 |
Journal | Fisheries Science |
Volume | 71 |
Issue number | 4 |
DOIs | |
Publication status | Published - 2005 Aug |
Keywords
- Acorn barnacle
- Biomineralization
- C-type lectin
- Glycopeptidase F
- Glycoprotein
- Lectin
- N-linked sugar chain
ASJC Scopus subject areas
- Aquatic Science