Franzén A, Björnsson S, Heinegård D
Biochem J. 1981 Sep 1;197(3):669-74. doi: 10.1042/bj1970669.
Cartilage proteoglycan aggregate formation was studied by zonal rate centrifugation in sucrose gradients. Proteoglycan aggregates, monomers and proteins could be resolved. It was shown that the optimal proportion of hyaluronic acid for proteoglycan aggregate formation was about 1% of proteoglycan dry weight. The reaggregation of dissociated proteoglycan aggregate A1 fraction was markedly concentration-dependent and even at 9 mg/ml only about 90% of the aggregates were reformed. The lowest proportion of link protein required for maximal formation of link-stabilized proteoglycan aggregates was 1.5% of proteoglycan dry weight. It was separately shown that link protein co-sedimented with the proteoglycan monomer. By competition with isolated hyaluronic acid-binding-region fragments, a proportion of the link proteins was removed from the proteoglycan monomers, indicating that the link protein binds to the hyaluronic acid-binding region of the proteoglycan monomer.
通过在蔗糖梯度中进行区带速率离心研究软骨蛋白聚糖聚集体的形成。蛋白聚糖聚集体、单体和蛋白质可以被分离。结果表明,蛋白聚糖聚集体形成的透明质酸最佳比例约为蛋白聚糖干重的1%。解离的蛋白聚糖聚集体A1组分的重新聚集明显依赖于浓度,即使在9mg/ml时,也只有约90%的聚集体重新形成。形成连接稳定的蛋白聚糖聚集体所需的连接蛋白的最低比例为蛋白聚糖干重的1.5%。另外还表明,连接蛋白与蛋白聚糖单体共同沉降。通过与分离的透明质酸结合区域片段竞争,一部分连接蛋白从蛋白聚糖单体中被去除,这表明连接蛋白与蛋白聚糖单体的透明质酸结合区域结合。