Kinne R W, Fisher L W
J Biol Chem. 1987 Jul 25;262(21):10206-11.
A keratan sulfate proteoglycan was isolated under denaturing conditions from the mineral compartment of rabbit cortical bone. This small proteoglycan (Kd = 0.39 on Superose 6, Mr approximately 20,000 on sodium dodecyl sulfate gels) contained small keratan sulfate chains that were distinctly bimodal in size. The keratanase and endo-beta-galactosidase digestible glycosaminoglycan chains were O-linked to a core protein of Mr approximately 80,000. This core protein had several properties in common with the bone sialoprotein II molecule of bovine and human bone including: a closely spaced doublet band on sodium dodecyl sulfate electrophoresis gels; a high staining intensity with Stains All that was greatly diminished by neuraminidase; a significant amount of small O-linked oligosaccharides; and an amino-terminal amino acid sequence that was nearly identical to human bone sialoprotein II. (In contrast, bone sialoprotein II in human, bovine, and rat bone does not appear to have any keratan sulfate chains.) Antiserum made against the keratan sulfate proteoglycan reacted with its core protein on electrotransfers from sodium dodecyl sulfate-polyacrylamide gels.
在变性条件下，从兔皮质骨的矿物质部分分离出一种硫酸角质素蛋白聚糖。这种小蛋白聚糖（在Superose 6上的Kd = 0.39，在十二烷基硫酸钠凝胶上的Mr约为20,000）含有大小明显呈双峰分布的小硫酸角质素链。可被角质酶和内切β - 半乳糖苷酶消化的糖胺聚糖链通过O - 连接与Mr约为80,000的核心蛋白相连。该核心蛋白具有与牛和人骨的骨唾液酸蛋白II分子相同的几个特性，包括：在十二烷基硫酸钠电泳凝胶上紧密间隔的双峰带；用甲酚紫染色时染色强度高，经神经氨酸酶处理后大大减弱；大量的小O - 连接寡糖；以及与人类骨唾液酸蛋白II几乎相同的氨基末端氨基酸序列。（相比之下，人、牛和大鼠骨中的骨唾液酸蛋白II似乎没有任何硫酸角质素链。）针对硫酸角质素蛋白聚糖制备的抗血清在从十二烷基硫酸钠 - 聚丙烯酰胺凝胶进行电转移时与其核心蛋白发生反应。
