DERMATAN SULFATE PROTEOGLYCANS OF HUMAN ARTICULAR-CARTILAGE - THE PROPERTIES OF DERMATAN SULFATE PROTEOGLYCAN-I AND PROTEOGLYCAN-II
DERMATAN SULFATE PROTEOGLYCANS OF HUMAN ARTICULAR-CARTILAGE - THE PROPERTIES OF DERMATAN SULFATE PROTEOGLYCAN-I AND PROTEOGLYCAN-II
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DOI：
10.1042/bj2620823
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发表时间：
1989-09-15
影响因子：
4.1
通讯作者：
WHITE, RJ
中科院分区：
文献类型：
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作者：
ROUGHLEY, PJ;WHITE, RJ
从幼年人关节软骨中纯化硫酸皮肤素蛋白聚糖，产率为约2 mg/g湿重。软骨组织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）均被鉴定，前者的丰度更高。这两种蛋白多糖不能用琼脂糖/聚丙烯酰胺凝胶电泳分离，但可以用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和DS-PGII的核心蛋白的Mr值分别为44000和43000和47000，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处存在用于硫酸皮肤素潜在取代的单个位点，并且在DS-PGI的残基5和10处存在两个这样的位点。
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 electrophoreis, 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.