Neame P J, Périn J P, Bonnet F, Christner J E, Jollès P, Baker J R
J Biol Chem. 1985 Oct 15;260(23):12402-4.
Cartilage proteoglycan monomers associate with hyaluronic acid to form proteoglycan aggregates. Link protein, interacting with both hyaluronic acid and proteoglycan, serves to stabilize the aggregate structure. In the course of determining the primary structure of link protein, two peptides produced by digestion of rat chondrosarcoma link protein with trypsin or chymotrypsin have been selectively purified by immunoaffinity chromatography on a column of monoclonal anti-link protein antibody (8A4) immobilized to Sepharose 4B. These peptides have been sequenced using the double-coupling dimethylaminoazobenzene isothiocyanate/phenyl isothiocyanate procedure. A consensus sequence, Cys-X-Ala-Gly-Trp-Leu-X-Asp-Gly-Ser-Val-X-Tyr-Pro-Ile-X-X-Pro, obtained by comparing the affinity-isolated tryptic peptide with the affinity-isolated chymotryptic peptide and an overlapping tryptic peptide, shows homology with a sequence obtained from the NH2-terminal of a CNBr peptide from proteo glycan core protein of bovine nasal cartilage: Ser-Ser-Ala-Gly-Trp-Leu-Ala-Asp-Arg-Ser-Val-Arg-Tyr-Pro-Ile-Ser-. We suggest that the common sequence is structurally important to the function of these proteins and may be involved in the binding of both link protein and proteoglycan to hyaluronic acid.
软骨蛋白聚糖单体与透明质酸结合形成蛋白聚糖聚集体。连接蛋白与透明质酸和蛋白聚糖相互作用，起到稳定聚集体结构的作用。在确定连接蛋白一级结构的过程中，通过固定在琼脂糖4B上的单克隆抗连接蛋白抗体（8A4）柱上的免疫亲和层析，选择性地纯化了用胰蛋白酶或糜蛋白酶消化大鼠软骨肉瘤连接蛋白产生的两种肽。这些肽已使用双偶联二甲基氨基偶氮苯异硫氰酸酯/苯异硫氰酸酯方法进行测序。通过将亲和分离的胰蛋白酶肽与亲和分离的糜蛋白酶肽以及一个重叠的胰蛋白酶肽进行比较，获得了一个共有序列：Cys-X-Ala-Gly-Trp-Leu-X-Asp-Gly-Ser-Val-X-Tyr-Pro-Ile-X-X-Pro，该序列与从牛鼻软骨蛋白聚糖核心蛋白的CNBr肽的NH2末端获得的序列具有同源性：Ser-Ser-Ala-Gly-Trp-Leu-Ala-Asp-Arg-Ser-Val-Arg-Tyr-Pro-Ile-Ser-。我们认为该共有序列在结构上对这些蛋白质的功能很重要，并且可能参与连接蛋白和蛋白聚糖与透明质酸的结合。
