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.

Source: Glycobiology - August 7, 2016 Category: Biology Authors: Fu, L., Sun, X., He, W., Cai, C., Onishi, A., Zhang, F., Linhardt, R. J., Liu, Z. Tags: Original articles Source Type: research