首页> 美国卫生研究院文献>Biochemical Journal >Dermatan sulphate proteoglycans of human articular cartilage. The properties of dermatan sulphate proteoglycans I and II.
【2h】

Dermatan sulphate proteoglycans of human articular cartilage. The properties of dermatan sulphate proteoglycans I and II.

机译:人关节软骨的硫酸皮肤素蛋白聚糖。硫酸皮肤素蛋白聚糖I和II的特性。

代理获取
本网站仅为用户提供外文OA文献查询和代理获取服务,本网站没有原文。下单后我们将采用程序或人工为您竭诚获取高质量的原文,但由于OA文献来源多样且变更频繁,仍可能出现获取不到、文献不完整或与标题不符等情况,如果获取不到我们将提供退款服务。请知悉。

摘要

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.
机译:从少年人关节软骨中纯化硫酸皮肤素蛋白聚糖,湿重约2mg / g。软骨。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)均已鉴定,并且前者的含量较高。两种蛋白聚糖不能通过琼脂糖/聚丙烯酰胺-凝胶电泳分离,但可以通过SDS /聚丙烯酰胺-凝胶电泳分离,这表明DS-PGI和DS-PGII的平均Mr值分别为200,000和98,000。用软骨素ABC裂解酶消化后,DS-PGI的核心蛋白的Mr值为44,000,DS-PGII的核心蛋白的Mr值为43,000和47,000,其中较小的核心蛋白在DS-PGII中占主导地位。 N末端20个氨基酸残基的序列分析揭示了在DS-PGII的残基4处存在潜在的硫酸皮肤素替代的单个位点以及在DS-PGI的残基5和10处存在两个此类位点。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
代理获取

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号