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从人关节软骨中分离蛋白聚糖。

Isolation of proteoglycans from human articular cartilage.

作者信息

Bayliss M T, Ali S Y

出版信息

Biochem J. 1978 Jan 1;169(1):123-32. doi: 10.1042/bj1690123.

Abstract

Proteoglycans were extracted from normal human articular cartilage of various ages with 4M-guanidinium chloride and were purified and characterized by using preformed linear CsCl density gradients. With advancing age, there was a decrease in high-density proteoglycans of low protein/uronic acid weight ratio and an increase in the proportion of lower-density proteoglycans, richer in keratan sulphate and protein. Proteoglycans of each age were also shown to disaggregate in 4M-guanidinium chloride and at low pH and to reaggregate in the presence of hyaluronic acid and/or low-density fractions. Osteoarthrotic-cartilage extracts had an increased content of higher-density proteoglycans compared with normal cartilage of the same age, and results also suggested that these were not mechanical or enzymic degradation products, but were possibly proteoglycans of an immature nature.

摘要

用4M氯化胍从不同年龄正常人关节软骨中提取蛋白聚糖,并用预制线性氯化铯密度梯度进行纯化和表征。随着年龄增长,低蛋白/糖醛酸重量比的高密度蛋白聚糖减少,硫酸角质素和蛋白质含量更高的低密度蛋白聚糖比例增加。每个年龄段的蛋白聚糖在4M氯化胍和低pH条件下也会解聚,并在透明质酸和/或低密度组分存在时重新聚集。与同年龄的正常软骨相比,骨关节炎软骨提取物中高密度蛋白聚糖的含量增加,结果还表明这些不是机械或酶促降解产物,而可能是未成熟性质的蛋白聚糖。

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