连接蛋白在软骨蛋白聚糖聚集体结构中的作用。
The role of link-protein in the structure of cartilage proteoglycan aggregates.
作者信息
Hardingham T E
出版信息
Biochem J. 1979 Jan 1;177(1):237-47. doi: 10.1042/bj1770237.
Proteoglycan fractions were prepared from pig laryngeal cartilage. The effect of link-protein on the properties of proteoglycan-hyaluronate aggregates was examined by viscometry and analytical ultracentrifugation. Aggregates containing link-protein were more stable than link-free aggregates at neutral pH, at temperatures up to 50 degrees C and in urea (up to 4.0M). Oligosaccharides of hyaluronate were able to displace proteoglycans from link-free aggregates, but not from the link-stabilized aggregates. Both types of aggregate were observed in the ultracentrifuge, but at the concentration investigated (less than 2 mg/ml) the link-free form was partially dissociated and the proportion aggregated varied with the pH and temperature and required more hyaluronate for saturation than did link-stabilized aggregate. The results showed that link-protein greatly strengthened the binding of proteoglycans to hyaluronate and suggest that under physiological conditions it 'locks' proteoglycans on to the hyaluronate chain.
从猪喉软骨中制备蛋白聚糖组分。通过粘度测定法和分析超速离心法研究了连接蛋白对蛋白聚糖 - 透明质酸聚集体性质的影响。在中性pH值、高达50摄氏度的温度以及尿素（高达4.0M）存在的情况下，含有连接蛋白的聚集体比不含连接蛋白的聚集体更稳定。透明质酸的寡糖能够从不含连接蛋白的聚集体中取代蛋白聚糖，但不能从连接蛋白稳定的聚集体中取代。在超速离心机中观察到了两种类型的聚集体，但在所研究的浓度（小于2mg/ml）下，不含连接蛋白的形式部分解离，聚集比例随pH值和温度而变化，并且与连接蛋白稳定的聚集体相比，达到饱和需要更多的透明质酸。结果表明，连接蛋白极大地增强了蛋白聚糖与透明质酸的结合，并表明在生理条件下它将蛋白聚糖“锁定”在透明质酸链上。
Zotero 插件