Matsue H, Takagaki K, Honda K, Endo M
Tohoku J Exp Med. 1985 Aug;146(4):391-400. doi: 10.1620/tjem.146.391.
Human urinary chondroitin sulfate isolated from the cetylpyridinium chloride-complex of the non-dialyzable fraction of the pooled urine was subjected to ethanol fractionation, successive enzymic digestion with neuraminidase and mucopolysaccharidases, and anion exchange chromatography. The gas liquid chromatographic analyses of the acetyl and butaneboronic acid ester derivatives of the reduced terminal sugar units after treatment with sodium borohydride plus hydrolysis revealed that 42% of the urinary chondroitin sulfate was bound to peptide through xylose. The reducing terminal sugar units of the peptide-free form consisted of 34.6% of xylose, 22.4% of galactose, 16.4% of glucose of unknown origin and 26.6% of glucuronic acid. These observations showed that the xyloside, galactoside and glucuronide linkages at non-terminal sites of carbohydrate chains of chondroitin sulfate were cleaved in tissues. It was thus suggested that the endo-types of beta-xylosidase, beta-galactosidase and beta-glucuronidase, which act on proteochondroitin sulfate are present in tissues.
从混合尿液不可透析部分的十六烷基氯化吡啶鎓复合物中分离出的人尿硫酸软骨素，经过乙醇分级分离、用神经氨酸酶和粘多糖酶进行连续酶消化以及阴离子交换色谱法处理。在用硼氢化钠处理并水解后，对还原末端糖单元的乙酰基和丁硼酸酸酯衍生物进行气液色谱分析，结果显示42%的尿硫酸软骨素通过木糖与肽结合。无肽形式的还原末端糖单元由34.6%的木糖、22.4%的半乳糖、16.4%来源不明的葡萄糖和26.6%的葡萄糖醛酸组成。这些观察结果表明，硫酸软骨素碳水化合物链非末端位点的木糖苷、半乳糖苷和葡萄糖醛酸苷键在组织中被裂解。因此提示，作用于硫酸蛋白软骨素的β-木糖苷酶、β-半乳糖苷酶和β-葡萄糖醛酸酶的内切型存在于组织中。
