Halberg D F, Proulx G, Doege K, Yamada Y, Drickamer K
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032.
J Biol Chem. 1988 Jul 5;263(19):9486-90.
A segment of 130 residues near the COOH terminus of the proteoglycan core protein derived from rat cartilage is highly homologous to the carbohydrate-recognition domain of the chicken hepatic lectin and other vertebrate carbohydrate-binding proteins. This portion of the protein has been expressed in an in vitro transcription and translation system and has been tested for its ability to interact with carbohydrates using affinity chromatography on immobilized sugars. A distinct specificity of the binding interaction is demonstrable, with fucose and galactose being the preferred ligands. However, the affinity of the expressed domain of the proteoglycan core protein is lower than that of the other known binding domains, since it elutes from the columns even in the presence of Ca2+.
源自大鼠软骨的蛋白聚糖核心蛋白COOH末端附近的一段130个残基的片段，与鸡肝凝集素和其他脊椎动物碳水化合物结合蛋白的碳水化合物识别结构域高度同源。该蛋白部分已在体外转录和翻译系统中表达，并使用固定化糖的亲和色谱法测试了其与碳水化合物相互作用的能力。结合相互作用具有明显的特异性，岩藻糖和半乳糖是优选的配体。然而，蛋白聚糖核心蛋白表达结构域的亲和力低于其他已知的结合结构域，因为即使在存在Ca2+的情况下它也会从柱上洗脱下来。
