Cardin A D, Jackson R L, Sparrow D A, Sparrow J T
Merrell Dow Research Institute, Cincinnati, Ohio 45215-6300.
Ann N Y Acad Sci. 1989;556:186-93. doi: 10.1111/j.1749-6632.1989.tb22503.x.
Apolipoproteins B-100 and E are protein constituents of human plasma chylomicrons, very low (VLDL), and low density lipoproteins (LDL). The interaction of lipoproteins with cell receptors is mediated by apoB and E. Lipoproteins also bind to the extracellular matrix, such as glycosaminoglycans (GAG), forming insoluble complexes in the presence of Ca2+. The purpose of this study was to identify the GAG-binding domains in apoB and E. By a combination of fragmentation of the intact proteins, peptide synthesis and quantitative GAG-binding, domains in apoB and apoE were identified and are shown below. These domains contain clusters of basic amino acids that we suggest are required for GAG-binding. table; see text.
载脂蛋白B-100和E是人类血浆乳糜微粒、极低密度脂蛋白（VLDL）和低密度脂蛋白（LDL）的蛋白质成分。脂蛋白与细胞受体的相互作用由载脂蛋白B和E介导。脂蛋白还与细胞外基质结合，如糖胺聚糖（GAG），在Ca2+存在下形成不溶性复合物。本研究的目的是鉴定载脂蛋白B和E中的GAG结合结构域。通过完整蛋白质的片段化、肽合成和定量GAG结合相结合的方法，鉴定出了载脂蛋白B和载脂蛋白E中的结构域，如下所示。这些结构域包含碱性氨基酸簇，我们认为这些簇是GAG结合所必需的。表；见正文。
