Characterisation of collagen from normal and scoliotic human spinal ligament.
Acid-soluble and pepsin-soluble collagens have been isolated from spinal ligaments of normal and scoliotic individuals. Polyacrylamide gel electrophoresis of native and cyanogen bromide-treated collagens, and amino acid analysis, showed that the ligament collagen is almost all of the Type I variety with only trace amounts of Type III present. There was no evidence for abnormal ratios of collagen alpha-chains, or underhydroxylation of proline and lysine in the scoliotic ligament. These results indicate that collagen biochemistry is normal with respect to type, post-translational modification and cross-linking in spinal ligaments of patients with idiopathic scoliosis. Elastin and proteoglycan were only minor components of the ligaments. The nature of the non-collagenous part of the ligament is unknown, although it contains some proteins with a hydrophobic nature.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D003094:Collagen / Q000032:analysis*; D003488:Cyanogen Bromide; D004549:Elastin / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D006603:Hexuronic Acids / Q000032:analysis; D006801:Humans; D010434:Pepsin A / Q000378:metabolism; D051381:Rats; D012600:Scoliosis / Q000473:pathology*; D013116:Spinal Cord / Q000032:analysis*
D000596:Amino Acids; D006603:Hexuronic Acids; D003094:Collagen; D004549:Elastin; D010434:Pepsin A; D003488:Cyanogen Bromide