Fransson L A, Carlstedt I, Cöster L, Malmström A
J Biol Chem. 1983 Dec 10;258(23):14342-5.
We have studied the affinity between fibroblast proteoheparan sulfate (medium- and cell surface-derived species) and heparan sulfate-agaroses by affinity chromatography. The evidence for an interaction between the heparan sulfate side chains of the proteoglycans and the immobilized heparan sulfate are as follows: (a) the individual side chains released from the proteoglycan by papain bind to the affinity matrix, (b) the bound proteoglycans are desorbed by a solution of cognate heparan sulfate chains, and (c) the core protein obtained by heparan sulfate-lyase digestion of the proteoglycan does not bind to the affinity matrix. The proteoglycans interact only with one subtype of heparan sulfate. The binding of free heparan sulfate chains to the affinity matrix is completely abolished by heparan sulfate oligosaccharides provided they are composed of both iduronate- and glucuronate-containing disaccharide sequences.
我们通过亲和色谱法研究了成纤维细胞蛋白聚糖硫酸乙酰肝素（源自培养基和细胞表面的种类）与硫酸乙酰肝素琼脂糖之间的亲和力。蛋白聚糖的硫酸乙酰肝素侧链与固定化硫酸乙酰肝素之间相互作用的证据如下：(a) 木瓜蛋白酶从蛋白聚糖释放的单个侧链与亲和基质结合；(b) 结合的蛋白聚糖被同源硫酸乙酰肝素链溶液解吸；(c) 用硫酸乙酰肝素裂解酶消化蛋白聚糖得到的核心蛋白不与亲和基质结合。这些蛋白聚糖仅与硫酸乙酰肝素的一种亚型相互作用。只要硫酸乙酰肝素寡糖由含艾杜糖醛酸和葡萄糖醛酸的二糖序列组成，游离硫酸乙酰肝素链与亲和基质的结合就会被完全消除。
