Vasan N
Biochem J. 1980 Jun 1;187(3):781-7. doi: 10.1042/bj1870781.
Proteoglycans from osteoarthritic cartilage were compared with those from normal articular cartilage. Normal proteoglycan aggregates are larger in size and more homogeneous than those in osteoarthritis. Proteoglycan monomers from both sources gave two peaks on controlled pore glass-bead chromatography. Although the retarded material from normal cartilage showed an affinity for hyaluronate, the same material from osteoarthritic cartilage did not. The hyaluronate-binding capacity of the material which is partly in the void volume and partly retarded was similar in both types of cartilage. These results suggest that in osteoarthritic cartilage the proteoglycan aggregates are smaller and more heterogeneous and that the chondroitin sulphate side chains are shorter. They also indicate that there are two populations of proteoglycan, one with its hyaluronate-binding-protein region of core protein intact and the other either possessing an inactive binding region or totally lacking it.
对骨关节炎软骨中的蛋白聚糖与正常关节软骨中的蛋白聚糖进行了比较。正常的蛋白聚糖聚集体在尺寸上更大，且比骨关节炎中的蛋白聚糖聚集体更均匀。来自这两种来源的蛋白聚糖单体在可控孔径玻璃珠色谱上都给出了两个峰。尽管来自正常软骨的滞留物质对透明质酸有亲和力，但来自骨关节炎软骨的相同物质却没有。在两种类型的软骨中，部分存在于空体积中且部分滞留的物质的透明质酸结合能力相似。这些结果表明，在骨关节炎软骨中，蛋白聚糖聚集体更小且更具异质性，硫酸软骨素侧链更短。它们还表明存在两种蛋白聚糖群体，一种其核心蛋白的透明质酸结合蛋白区域完整，另一种要么具有无活性的结合区域，要么完全缺乏该区域。
