Matrix sialoprotein of developing bone.

The effect of changes in endolymphatic ion concentrations on the tectorial membrane.

CHAPTER 5 – The Organic Matrix of Bone

Glycoproteins of the connective tissue matrix.

http://doras.dcu.ie/17772/2/ELLA_2011.pdf

Optimization of the enzyme-linked lectin assay for enhanced glycoprotein and glycoconjugate analysis.

1. Bovine bone sialoprotein (mol.wt. 23000) contains N-acetylneuraminic acid and N-glycollylneuraminic acid, fucose, galactose, mannose, N-acetylgalactosamine and N-acetylglucosamine residues in the form of a very small number, perhaps one, of highly branched oligosaccharide structures linked covalently to peptide. 2. Periodate oxidation of the sialoprotein results in quantitative destruction only of the sialic acid and fucose residue consistent with the earlier findings of their positions as terminal groups. 3. Terminal sialic acid residues are attached to galactopyranose residues by 2,3-linkages, and to some N-acetylgalactosamine residues (at C-6). 4. Sequential Smith degradation indicates that N-acetylgalactosamine residues may be present as points of branching (linked in C-1, C-3 and C-6) and N-acetylglucosamine residues are located in the inner part of the structure, adjacent to the carbohydrate–peptide bond(s). 5. Mannose residues appear to be linked in the 1,3-positions.

A. T. De B. Andrews

Papers

The periodate oxidation of bovine bone sialoprotein, and some observations on its structure.