Shogren R L, Jentoft N, Gerken T A, Jamieson A M, Blackwell J
Carbohydr Res. 1987 Feb 15;160:317-27. doi: 10.1016/0008-6215(87)80320-8.
Static and dynamic light-scattering studies of solutions of ovine submaxillary mucin (OSM) glycoproteins, fractionated by exclusion chromatography on Sephacryl S-1000, are reported. These experiments yielded information regarding the structure and conformation of the glycoprotein chain, in the form of weight-average molecular weights, Mw, z-average radius of gyration, Rg,z, and z-average of the inverse hydrodynamic radius, (Rh-1)z. The values of (Rh-1)z are found to correlate very well with the S-1000 elution volume characteristics for four OSM fractions of different molecular weights. The structural parameters for these OSM fractions are, within experimental error, similar to those deduced for porcine submaxillary mucins (PSM) in earlier studies. The results suggest that, like PSM, the glycoprotein structure of OSM consists of linear chains constructed by covalently linking two or more elementary subunits together via disulfide bonds. In addition, the rigidity of the protein core of OSM is substantially greater than that observed for non-glycosylated-polypeptide random coils. Because (Rh-1)z, and hence, elution volume depends only on the molecular weight of the mucin protein core, the Mw calibration obtained for OSM should be applicable to the chromatography of other mucin glycoproteins.
报道了对经Sephacryl S - 1000排阻色谱分级分离的绵羊下颌粘蛋白（OSM）糖蛋白溶液进行的静态和动态光散射研究。这些实验以重均分子量Mw、z - 平均回转半径Rg,z和反流体力学半径的z - 平均（Rh-1）z的形式，得出了有关糖蛋白链结构和构象的信息。发现（Rh-1）z的值与四种不同分子量的OSM级分的S - 1000洗脱体积特征非常好地相关。在实验误差范围内，这些OSM级分的结构参数与早期研究中推导的猪下颌粘蛋白（PSM）的结构参数相似。结果表明，与PSM一样，OSM的糖蛋白结构由通过二硫键将两个或更多基本亚基共价连接在一起构成的线性链组成。此外，OSM蛋白质核心的刚性明显大于非糖基化多肽无规卷曲所观察到的刚性。由于（Rh-1）z以及洗脱体积仅取决于粘蛋白蛋白质核心的分子量，因此为OSM获得的Mw校准应适用于其他粘蛋白糖蛋白的色谱分析。
