Link-proteins and non-collagenous proteins from normal and chondrodysplastic cartilages.
Baboon and human articular and growth cartilage was extracted with 4M guanidinium chloride in the presence of proteolysis inhibitors. After dialysis against 8M urea pH 6.8 the proteins were separated from proteoglycans by ion-exchange chromatography. The concentrated and reduced protein fractions was analyzed by SDS-PAGE. Bands corresponding to collagen and to 6 major non-collegenous proteins were found. Two of the latter were identified with the link-proteins. By using small columns and microconcentration procedures, a gel-electrophoretic analysis of link-proteins extracted from small pieces of cartilage was performed and ten cases of osteochondrodysplasias were studied. No abnormalities were detected in the following syndromes: achondroplasia, diastrophic dwarfism, thanatophoric dwarfism, Jeune disease, spondyloepiphyseal dysplasia congenita, Kozlowski syndrome, osteogenesis imperfecta, polyepiphyseal dysplasia with diabetes mellitus.
D000130:Achondroplasia / Q000473:pathology; D000293:Adolescent; D000818:Animals; D002356:Cartilage / Q000032:analysis*; D002358:Cartilage, Articular / Q000032:analysis; D002648:Child; D002675:Child, Preschool; D003094:Collagen / Q000032:analysis; D004392:Dwarfism / Q000473:pathology; D000882:Haplorhini; D006801:Humans; D007231:Infant, Newborn; D010009:Osteochondrodysplasias / Q000473:pathology*; D010013:Osteogenesis Imperfecta / Q000473:pathology; D010215:Papio; D011506:Proteins / Q000032:analysis*
D011506:Proteins; D003094:Collagen