Klein U, von Figura K
Hoppe Seylers Z Physiol Chem. 1979 Oct;360(10):1465-71. doi: 10.1515/bchm2.1979.360.2.1465.
A heparan sulfate-degrading endoglucuronidase was isolated from human placenta and partially purified by affinity chromatography on heparan sulfate-Sepharose 4B. The endoglucuronidase has a molecular weight of approximately 100 000 estimated by gel chromatography and a broad pH optimum between pH4 and pH6. Carboxyl reduced heparan sulfate is not split by partially purified endoglucuronidase, but inhibits the action of that enzyme towards non-modified heparan sulfate. Low molecular weight heparan sulfate (Mr approximately 3 000) is not attacked by the endoglucuronidase. N-Desulfated heparan sulfate and heparin are only weak substrates. The amino sugar adjacent to the glucuronic acid residue appearing at the reducing terminal of heparan sulfate fragments liberated by the endoglucuronidase appears to be exclusively N-acetylated glucosamine.
从人胎盘中分离出一种硫酸乙酰肝素降解性内切葡糖醛酸酶，并通过在硫酸乙酰肝素 - 琼脂糖4B上进行亲和层析进行部分纯化。通过凝胶色谱法估计，该内切葡糖醛酸酶的分子量约为100000，在pH4至pH6之间具有较宽的最适pH值。羧基还原的硫酸乙酰肝素不能被部分纯化的内切葡糖醛酸酶裂解，但会抑制该酶对未修饰硫酸乙酰肝素的作用。低分子量硫酸乙酰肝素（Mr约为3000）不会被内切葡糖醛酸酶攻击。N - 去硫酸化硫酸乙酰肝素和肝素只是较弱的底物。内切葡糖醛酸酶释放的硫酸乙酰肝素片段还原末端出现的与葡糖醛酸残基相邻的氨基糖似乎仅为N - 乙酰化葡糖胺。
