Sandy J D, Plaas A H
Biochem J. 1985 Dec 1;232(2):613-6. doi: 10.1042/bj2320613.
A new assay for the activity of cartilage link protein is described. The method is based on the finding [Plaas, Sandy & Muir (1983) Biochem. J. 214, 855-864] that addition of link protein to [35S]sulphate-labelled proteoglycan aggregates from rabbit chondrocyte cultures resulted in the formation of link-stabilized aggregates. The percentage aggregate was found to be related linearly to the amount of purified bovine link protein added in the 20-120 ng range. The assay was used to monitor loss of link-protein activity during heat denaturation and to measure binding of link protein by purified proteoglycan monomer.
本文描述了一种用于检测软骨连接蛋白活性的新方法。该方法基于以下发现[普拉斯、桑迪和缪尔（1983年），《生物化学杂志》214卷，第855 - 864页]：向来自兔软骨细胞培养物的[35S]硫酸盐标记的蛋白聚糖聚集体中添加连接蛋白会导致形成连接稳定的聚集体。发现在20 - 120纳克范围内，聚集体的百分比与添加的纯化牛连接蛋白的量呈线性关系。该检测方法用于监测热变性过程中连接蛋白活性的丧失，并测量纯化的蛋白聚糖单体与连接蛋白的结合。
