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利用两种抗分子量为２４０００的血小板膜糖蛋白的单克隆抗体（ＭｃＡｂ）为探针，对血小板活化进行研究。结果显示：两种ＣＤ９ＭｃＡｂ（ＳＪ９Ａ４，ＨＩ１１７）在其抗原（Ｐ２４）上的识别肽段不同；两种ＭｃＡｂ诱聚血小板的途径有区别；在激活血小板时，两种ＭｃＡｂ能同时引发特定的血小板膜蛋白磷酸化，但ＨＩ１１７不能使血小板胞浆钙离子浓度升高；活化血小板Ｐ２４不能与膜上其他蛋白发生物理联结。表明两种ＣＤ９ＭｃＡｂ激活血小板的机理存在差异，提示其抗原在血小板活化中的作用是一个多方面的综合过程。
Platelet activation was investigated using two monoclonal antibodies (McAbs) against the platelet membrane glycoprotein of 24,000. The results showed that the recognition peptides of the two CD9McAb (SJ9A4, HI117) on their antigen (P24) were different. The two McAbs induced platelet aggregation differently. When activating platelets, both McAbs simultaneously induced specific platelet membrane Protein phosphorylation, but HI117 can not increase the concentration of platelet cytoplasmic calcium; activated platelet P24 can not be physically associated with other proteins on the membrane. This suggests that there are differences in the mechanism of action of two CD9McAb-activated platelets, suggesting that the antigen’s role in platelet activation is a multifaceted and comprehensive process.