Axelsson I, Bjelle A
Scand J Rheumatol. 1979;8(4):217-21. doi: 10.3109/03009747909114626.
Proteoglycan subunits (PGS) were isolated from bovine articular cartilage of calves and from cows, 18 months and 8 years old respectively. From the latter cartilage of osteoarthrotic and of non-osteoarthrotic sites was taken. PGS were characterized by gel-chromatography on Sepharose 2B columns and subjected to digestion with chondroitinase ABC and with papain. The isolated keratan sulphate-protein cores obtained from chondroitinase digestion were characterized on Sepharose 4B and the chondroitin sulphate chains on Sephadex G-200 gels. A larger molecular size of PGS was found in calf cartilage than in the other samples. This was attributed to the larger molecular size of chondroitin, whereas no change was observed in the keratan sulphate-protein cores. No change was observed in molecular size of PGS, isolated chondroitin sulphates or keratan sulphate-protein cores in osteoarthrosis in comparison with non-osteoarthrotic cartilage from the same joint or from younger adult animals.
蛋白聚糖亚基（PGS）分别从小牛以及18个月和8岁母牛的牛关节软骨中分离得到。后者取自骨关节炎部位和非骨关节炎部位的软骨。通过在琼脂糖2B柱上进行凝胶色谱对PGS进行表征，并使用软骨素酶ABC和木瓜蛋白酶进行消化。从软骨素酶消化中获得的分离出的硫酸角质素-蛋白核心在琼脂糖4B上进行表征，硫酸软骨素链在葡聚糖G-200凝胶上进行表征。发现小牛软骨中的PGS分子大小比其他样品中的更大。这归因于软骨素分子大小更大，而硫酸角质素-蛋白核心未观察到变化。与来自同一关节或年轻成年动物的非骨关节炎软骨相比，骨关节炎中分离出的PGS、硫酸软骨素或硫酸角质素-蛋白核心的分子大小未观察到变化。
