Structural analysis of human platelet membrane glycoprotein I complex.
Structural analysis of human platelet membrane glycoprotein I complex.
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人血小板膜糖蛋白 I 复合物的结构分析。
DOI：
10.1073/pnas.76.6.2952
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发表时间：
1979
影响因子：
11.1
通讯作者：
B. Ferris
中科院分区：
文献类型：
--
作者：
R. Nachman;T. Kinoshita;B. Ferris
利用小麦胚芽凝集素亲和层析技术，从人血小板膜中分离到由Mr为21万和15万的两个多肽组成的糖蛋白I复合物。糖钙素是一种可溶性松散结合膜糖蛋白，Mr为150,000，与糖蛋白I系统有关。分离得到的多肽在十二烷基硫酸钠/聚丙烯酰胺凝胶中放射性碘化，胰蛋白酶消化，用二维高压电泳和薄层色谱分析标记的肽消化。糖蛋白I复合体中Mr 210,000和Mr 150,000的两个多肽具有本质上相同的放射性肽图。糖钙蛋白有一个完全不同的色氨酸图。这些研究揭示了血小板膜糖蛋白I系统的一些组分的分子关系。提出了血小板膜糖蛋白的受体样功能可能与组成多肽的聚合亚基结合有关。
The glycoprotein I complex, consisting of two polypeptides of Mr 210,000 and 150,000, was isolated from human platelet membranes by wheat germ lectin affinity chromatography. Glycocalicin, a soluble loosely bound membrane glycoprotein of Mr 150,000 related to the glycoprotein I system, was also purified. The isolated polypeptides were radioiodinated in sodium dodecyl sulfate/polyacrylamide gels and digested with trypsin, and the labeled peptide digest was analyzed by two-dimensional high-voltage electrophoresis and thin-layer chromatography. The two polypeptides of Mr 210,000 and 150,000 in the glycoprotein I complex had essentially identical radioactive peptide maps. Glycocalicin had a completely different tryptic peptide map. These studies shed light on the molecular relationships of some of the components of the platelet membrane glycoprotein I system. The possibility is raised that the receptorlike function of the intrinsic platelet membrane glycoproteins may be related to the polymeric subunit associations of the constituent polypeptides.