Clemetson K J, Bienz D, Zahno M L, Lüscher E F
Biochim Biophys Acta. 1984 Dec 19;778(3):463-9. doi: 10.1016/0005-2736(84)90395-x.
Platelets, either unlabelled, surface-labelled by the periodate NaB3H4 method or metabolically labelled with 32P were solubilized in Triton X-114 and partitioned into aqueous and detergent phases. The phases were analysed by two-dimensional polyacrylamide gel electrophoresis followed by silver-staining, fluorography or indirect autoradiography. Each of the phases contains a distinct set of proteins. The surface-labelled glycoproteins partition into the hydrophobic phase with the notable exceptions of glycoproteins Ib and GP17(5.8-6.5) and minor amounts of a few others. The phosphoproteins which undergo increased phosphorylation on platelet activation in general separate in the hydrophobic phase, while higher molecular weight phosphoproteins were principally in the hydrophilic phase. This method might be used as a first step in purifying many platelet components.
血小板，无论是未标记的、通过高碘酸钠硼氢化钠（NaB3H4）法进行表面标记的，还是用32P进行代谢标记的，都在Triton X-114中溶解，并被分配到水相和去污剂相中。通过二维聚丙烯酰胺凝胶电泳，随后进行银染、荧光显影或间接放射自显影来分析这些相。每个相中都含有一组独特的蛋白质。表面标记的糖蛋白会分配到疏水相中，但糖蛋白Ib和GP17（5.8 - 6.5）以及少量其他糖蛋白是明显的例外。在血小板活化时磷酸化增加的磷蛋白通常在疏水相中分离，而高分子量的磷蛋白主要存在于亲水相中。这种方法可作为纯化许多血小板成分的第一步。
