Roughley P J, White R J
Joint Diseases Laboratory, Shriners Hospital for Crippled Children, Montreal, Quebec, Canada.
Biochem J. 1989 Sep 15;262(3):823-7. doi: 10.1042/bj2620823.
Dermatan sulphate proteoglycans were purified from juvenile human articular cartilage, with a yield of about 2 mg/g wet wt. of cartilage. Both dermatan sulphate proteoglycan I (DS-PGI) and dermatan sulphate proteoglycan II (DS-PGII) were identified and the former was present in greater abundance. The two proteoglycans could not be resolved by agarose/polyacrylamide-gel electrophoresis, but could be resolved by SDS/polyacrylamide-gel electrophoresis, which indicated average Mr values of 200,000 and 98,000 for DS-PGI and DS-PGII respectively. After digestion with chondroitin ABC lyase the Mr values of the core proteins were 44,000 for DS-PGI and 43,000 and 47,000 for DS-PGII, with the smaller core protein being predominant in DS-PGII. Sequence analysis of the N-terminal 20 amino acid residues reveals the presence of a single site for the potential substitution of dermatan sulphate at residue 4 of DS-PGII and two such sites at residues 5 and 10 for DS-PGI.
从青少年人关节软骨中纯化出硫酸皮肤素蛋白聚糖,每克湿重软骨的产量约为2毫克。鉴定出了硫酸皮肤素蛋白聚糖I(DS-PGI)和硫酸皮肤素蛋白聚糖II(DS-PGII),且前者含量更高。这两种蛋白聚糖不能通过琼脂糖/聚丙烯酰胺凝胶电泳分离,但能通过SDS/聚丙烯酰胺凝胶电泳分离,这表明DS-PGI和DS-PGII的平均分子量分别为200,000和98,000。用软骨素ABC裂解酶消化后,DS-PGI核心蛋白的分子量为44,000,DS-PGII核心蛋白的分子量为43,000和47,000,较小的核心蛋白在DS-PGII中占主导。对N端20个氨基酸残基的序列分析表明,DS-PGII的第4位残基存在一个硫酸皮肤素潜在取代位点,DS-PGI的第5位和第10位残基存在两个这样的位点。