Structural varieties of small proteoglycans in human spinal ligament

Three types of small proteoglycan were purified from human spinal ligaments by ultracentrifugation, ion-exchange chromatography, gel-chromatography, a nd hydrophobic chromatography. Two of them were identified as decorin and b iglycan, and the other was thought to be a decorin-subtype. Molecular sizes of decorin and decorin-subtype were both 85 kDa, and that of biglycan was 200 kDa. N-Terminal amino acid sequence of decorin-subtype corresponded wit h that of decorin, although it was different from decorin in terms of compo sition of amino acids and glycosaminoglycan chains, and reactivity with ant i-human decorin antibody. The ratios of chondroitin sulfate to dermatan sul fate contained in the three proteoglycans were different, and the location of that in glycosaminoglycan chains was also thought to be different. It wa s demonstrated that three types of proteoglycan which are structurally diff erent are present in extracellular matrix.