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牛血中低硫酸化硫酸软骨素4-硫酸酯蛋白聚糖的分离及部分特性研究

Isolation and partial characterization of low sulfated chondroitin 4-sulfate-proteoglycan in bovine blood.

作者信息

Nakamura H, Nagai Y

出版信息

Biochim Biophys Acta. 1979 Feb 26;576(2):361-71. doi: 10.1016/0005-2795(79)90411-2.

DOI:10.1016/0005-2795(79)90411-2
PMID:427193
Abstract

Bovine plasma low sulfated chondroitin sulfate-proteoglycan (34 microgram/ml plasma), accounting for the main component of acidic glycosaminoglycans in blood, has been purified by isoelectric precipitation, dissociation with 4 M guanidine chloride followed by DEAE-chromatography, Sephadex G-200 chromatography and by preparative polyacrylamide gel electrophoresis. The proteoglycan, having a molecular weight of approx. 44,000, is composed of about 77% protein and 23% glycosaminoglycan at a molar ratio of 1 : 1 which could be cleaved by alkaline treatment into each component. Amino acid analysis of the proteoglycan and its glycosylpeptide has shown that the material is derived from a different origin from other tissue proteoglycans, though the amino acid residues surrounding O-glycosidic linkage to serine residue are quite similar to that of cartilage proteoglycan. Characteristic features of plasma low sulfate chondroitin sulfate-proteoglycan are discussed, compared with tissue materials.

摘要

牛血浆低硫酸化硫酸软骨素蛋白聚糖(34微克/毫升血浆)是血液中酸性糖胺聚糖的主要成分,已通过等电沉淀、用4M氯化胍解离,随后进行DEAE-色谱、Sephadex G-200色谱和制备性聚丙烯酰胺凝胶电泳进行了纯化。该蛋白聚糖的分子量约为44,000,由约77%的蛋白质和23%的糖胺聚糖组成,摩尔比为1:1,可通过碱性处理裂解为各组分。对该蛋白聚糖及其糖基肽的氨基酸分析表明,尽管与丝氨酸残基的O-糖苷键周围的氨基酸残基与软骨蛋白聚糖非常相似,但该物质的来源与其他组织蛋白聚糖不同。与组织材料相比,讨论了血浆低硫酸化硫酸软骨素蛋白聚糖的特征。

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