Anderson J C
Biochim Biophys Acta. 1975 Feb 27;379(2):444-55. doi: 10.1016/0005-2795(75)90151-8.
A fraction was isolated from a 3 M MgCl2 extract of bovine achilles tendon on the basis of its affinity for collagen. Affinity chromatography of this material on concanavalin A-Sepharose yielded a mixture which comprised a glycoprotein of approximate molecular weight 60 000 and two constituents containing hexuronic acid. The existence of a complex between the glycoprotein and material containing hexuronic acid was demonstrated by chromatography on Sephadex G-200 and by equilibrium sedimentation in CsCl density gradients. The complex was completely dissociated in 4 M guanidinium chloride. One of the constituents containing hexuronic acid was identified as a proteodermatan sulphate of low molecular weight and which had an abnormally high protein content (45-50%) and low buoyant density (1.46 g/ml) for a proteoglycan. The denser of the two molecules containing hexuronic acid appeared to be a normal proteoglycan, with a low protein content (11%). Analyses are given for the glycoprotein and the proteodermatan sulphate.
基于对胶原蛋白的亲和力，从牛跟腱的3M氯化镁提取物中分离出一种组分。该物质在伴刀豆球蛋白A - 琼脂糖上进行亲和层析，得到一种混合物，其中包括一种分子量约为60000的糖蛋白和两种含己糖醛酸的成分。通过在葡聚糖G - 200上的层析以及在氯化铯密度梯度中的平衡沉降，证明了糖蛋白与含己糖醛酸的物质之间存在复合物。该复合物在4M氯化胍中完全解离。其中一种含己糖醛酸的成分被鉴定为低分子量的蛋白皮肤素硫酸盐，对于蛋白聚糖而言，其蛋白质含量异常高（45 - 50%）且浮力密度低（1.46 g/ml）。两种含己糖醛酸的分子中密度较大的似乎是一种正常的蛋白聚糖，蛋白质含量低（11%）。文中给出了对糖蛋白和蛋白皮肤素硫酸盐的分析。
