COLLAGEN-PROTEIN-POLYSACCHARIDE INTERACTIONS IN HUMAN INTERVERTEBRAL DISC

The collagen-protein-polysaccharide complex present in human intervertebral disc has been prepared. Normal chromatographic separation techniques failed to fractionate this complex into pure collagen (or derived gelatin) and pure protein-polysaccharide complex. Fractionation was achieved by use of cetyltrimethylammonium bromide (CTAB)-cellulose chromatography. Selective binding of certain peptide fragments within the collagen polypeptide chains to the protein-polysaccharide complex was demonstrated by a combination of collagenase digestion, CTAB-cellulose chromatography and peptide fingerprinting studies. It is concluded that the stability of the collagen-protein polysaccharide complex is due to ionic interaction between the positively charged amino groups on the collagen and the negatively charged sulphonic acid groups on the protein polysaccharide complex, rather than to covalent bonds between these two components. The role of the intact protein core of the protein polysaccharide complex is also discussed. © 1969.