Keratan sulfate glycosaminoglycan from chicken egg white.


Keratan sulfate (KS) was isolated from chicken egg white in amounts corresponding to ∼0.06 wt% (dry weight). This KS had a weight-average molecular weight of ∼36-41 kDa with a polydispersity of ∼1.3. The primary repeating unit present in chicken egg white KS was →4) β-N-acetyl-6-O-sulfo-d-glucosamine (1 → 3) β-d-galactose (1→ with some 6-O-sulfo galactose residues present. This KS was somewhat resistant to depolymerization using keratanase 1 but could be depolymerized efficiently through the use of reactive oxygen species generated using copper (II) and hydrogen peroxide. Of particular interest was the presence of substantial amounts of 2,8- and 2,9-linked N-acetylneuraminic acid residues in the form of oligosialic acid terminating the non-reducing ends of the KS chains. Most of the KS appears to be N-linked to a protein core as evidenced by its sensitivity to PNGase F.

DOI: 10.1093/glycob/cww017

Cite this paper

@article{Fu2016KeratanSG, title={Keratan sulfate glycosaminoglycan from chicken egg white.}, author={Li Fu and Xiaojun Sun and Wenqin He and Chao Cai and Akihiro Onishi and Fuming Zhang and Robert J. Linhardt and Zhangguo Liu}, journal={Glycobiology}, year={2016}, volume={26 7}, pages={693-700} }