COPOLYMERIC STRUCTURE OF PIG SKIN DERMATAN SULFATE - ISOLATION AND CHARACTERIZATION OF L-IDURONO-SULPHATE-CONTAINING OLIGOSACCHARIDES FROM COPOLYMERIC CHAINS
COPOLYMERIC STRUCTURE OF PIG SKIN DERMATAN SULFATE - ISOLATION AND CHARACTERIZATION OF L-IDURONO-SULPHATE-CONTAINING OLIGOSACCHARIDES FROM COPOLYMERIC CHAINS
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DOI：
10.1042/bj1430379
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发表时间：
1974-01-01
影响因子：
4.1
通讯作者：
SJOBERG, I
中科院分区：
文献类型：
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作者：
FRANSSON, LA;COSTER, L;SJOBERG, I
硫酸皮肤素被睾丸透明质酸酶降解，并通过离子交换色谱法分离出过硫酸化部分。该制剂含有来自分子非还原性末端部分的相当长的片段，在酸性条件下进行高碘酸盐氧化。氧化的艾杜糖醛酸残基通过还原-水解（Smith降解）（Fransson & Carlstedt，1974）或碱消除进行裂解。如此获得的寡糖含有GlcUA（葡萄糖醛酸）和IdUA-SO 4（硫酸化艾杜糖醛酸）残基。用软骨素酶-AC将碱消除后得到的共聚物低聚糖裂解为二糖和更高级的低聚糖。由于通过Smith降解获得的相应寡糖不受该酶的影响，因此得出结论，碳水化合物序列为GalNAc-（IdUA-GalNAc）n-GlcUA-GalNAc。含艾杜糖醛酸的序列对软骨素酶-ABC消化具有抗性。结果表明，这些序列中存在未硫酸化的N-乙酰半乳糖胺残基可能是观察到的效果的原因。这些信息是间接获得的。发现化学磷酸化的硫酸皮肤素是软骨素酶-ABC酶的不良底物。此外，用软骨素酶-ABC消化软骨素酶-AC降解的硫酸皮肤素，释放出耐高过硫酸盐的含艾杜糖醛酸的低聚糖。得出结论，猪皮硫酸皮肤素中存在以下结构的共聚物序列：[分子式：见正文] IdUA-SO 4残基周围的N-乙酰半乳糖胺部分在很大程度上未硫酸化。
Dermatan sulphate was degraded by testicular hyaluronidase and an oversulphated fraction was isolated by ion-exchange chromatography. This preparation, which contained fairly long segments derived from the non-reducing terminal portion of the molecule, was subjected to periodate oxidation under acidic conditions. The oxidized iduronic acid residues were cleaved by reduction-hydrolysis (Smith-degradation) (Fransson & Carlstedt, 1974) or by alkaline elimination. The oligosaccharides so obtained contained both GlcUA (glucuronic acid) and IdUA-SO4(sulphated iduronic acid) residues. Copolymeric oligosaccharides obtained after alkaline elimination were cleaved by chondroitinase-AC into disaccharide and higher oligosaccharides. Since the corresponding oligosaccharides obtained by Smith-degradation were unaffected by this enzyme, it was concluded that the carbohydrate sequences were GalNAc-(IdUA-GalNAc)n-GlcUA-GalNAc. The iduronic acid-containing sequences were resistant to digestion with chondroitinase-ABC. It was demonstrated that the presence of unsulphatedN-acetylgalactosamine residues in these sequences could be responsible for the observed effect. This information was obtained in an indirect way. Chemically desulphated dermatan sulphate was found to be a poor substrate for the chondroitinase-ABC enzyme. Moreover, digestion with chondroitinase-ABC of chondroitinase-AC-degraded dermatan sulphate released periodate-resistant iduronic acid-containing oligosaccharides. It is concluded that copolymeric sequences of the following structure are present in pig skin dermatan sulphate: [Formula: see text]N-acetylgalactosamine moieties surrounding IdUA-SO4residues are unsulphated to a large extent.