Lewandrowski U, Zahedi R P, Moebius J, Sickmann A
Rudolf-Virchow-Zentrum für Experimentelle Biomedizin, Universität Würzburg.
Hamostaseologie. 2007 Sep;27(4):241-5.
Platelets are anucleated cells and therefore ideal research objects for modern proteome analyses. Despite their importance in thrombosis and hemostasis the protein content of platelets is still poorly characterized in major parts. In preparation for bioinformatic and functional studies a series of proteomic analyses was conducted for platelet subproteomes as well as for posttranslational modifications. Thereby, the identification of 489 proteins, over 550 phosphorylations and 326 N-glycosylation sites was possible, which were not identified in previous proteome studies of platelets. Those results represent new research possibilities for functional characterization of platelet proteins as well as their modifications.
血小板是无核细胞,因此是现代蛋白质组分析的理想研究对象。尽管血小板在血栓形成和止血过程中具有重要作用,但其蛋白质含量在很大程度上仍未得到充分表征。为了开展生物信息学和功能研究,对血小板亚蛋白质组以及翻译后修饰进行了一系列蛋白质组分析。由此,有可能鉴定出489种蛋白质、550多个磷酸化位点和326个N-糖基化位点,这些在以往血小板蛋白质组研究中均未被鉴定出来。这些结果为血小板蛋白质及其修饰的功能表征提供了新的研究可能性。