DiCesare P E, Mörgelin M, Mann K, Paulsson M
Cartilage and Bone Research Center, Hospital for Joint Diseases Orthopaedic Institute, New York, NY 10003.
Eur J Biochem. 1994 Aug 1;223(3):927-37. doi: 10.1111/j.1432-1033.1994.tb19070.x.
Cartilage oligomeric matrix protein (COMP) and thrombospondin 1 (TSP1) were purified in a native form from normal bovine articular cartilage. The key step in the purification scheme was selective extraction with EDTA-containing buffer. Final separation of these two molecules was achieved by heparin affinity chromatography. Particles viewed by electron microscopy after rotary shadowing and negative staining revealed structures similar to their prototype molecules; from the Swarm rat chondrosarcoma for COMP, or from platelets for TSP1. Attachment of primary bovine chondrocytes to purified matrix proteins was investigated. Cells attached to COMP but not to the structurally related TSP1 indicating separate functions for these proteins in cartilage.
从正常牛关节软骨中以天然形式纯化出软骨寡聚基质蛋白（COMP）和血小板反应蛋白1（TSP1）。纯化方案中的关键步骤是用含乙二胺四乙酸（EDTA）的缓冲液进行选择性提取。这两种分子的最终分离通过肝素亲和层析实现。旋转阴影和负染后通过电子显微镜观察到的颗粒显示出与其原型分子相似的结构；COMP的原型分子来自Swarm大鼠软骨肉瘤，TSP1的原型分子来自血小板。研究了原代牛软骨细胞与纯化的基质蛋白的附着情况。细胞附着于COMP，而不附着于结构相关的TSP1，表明这些蛋白在软骨中具有不同的功能。
