Nakano T, Scott P G
Department of Oral Biology, University of Alberta, Edmonton, Canada.
Matrix. 1989 Aug;9(4):277-83. doi: 10.1016/s0934-8832(89)80023-x.
Proteoglycans were extracted from articular discs with 4 M guanidinium chloride and separated by ion-exchange and gel-filtration chromatography into high molecular weight (Mr greater than 1,000,000) species containing chondroitin sulphate (predominantly chondroitin 6-sulphate) and low molecular weight iduronic acid-rich dermatan sulphate proteoglycan(s). The chondroitin sulphate proteoglycan contained 21% uronic acid and 17% protein. It gave rise on digestion with chondroitinase ABC to a protein core of apparent Mr 350,000 with an amino acid composition closely resembling that of the cartilage-type proteoglycans. Other characteristics shared with previously-described cartilage proteoglycans include the presence of keratan sulphate and the ability to aggregate with hyaluronic acid.
用4M氯化胍从关节盘中提取蛋白聚糖，并通过离子交换和凝胶过滤色谱法将其分离为含有硫酸软骨素（主要是硫酸软骨素6-硫酸盐）的高分子量（Mr大于1,000,000）物质和低分子量富含艾杜糖醛酸的硫酸皮肤素蛋白聚糖。硫酸软骨素蛋白聚糖含有21%的糖醛酸和17%的蛋白质。用软骨素酶ABC消化后，产生了一个表观Mr为350,000的蛋白核心，其氨基酸组成与软骨型蛋白聚糖非常相似。与先前描述的软骨蛋白聚糖共有的其他特征包括硫酸角质素的存在以及与透明质酸聚集的能力。
