Furlan M, Horisberger M, Perret B A, Beck E A
Br J Haematol. 1981 Jun;48(2):319-24. doi: 10.1111/j.1365-2141.1981.tb08465.x.
Platelet aggregating factor (PAF) activity is preferentially associated with the larger molecular forms of bovine factor VIII and diminishes considerably after dissociation into smaller oligomers by mild disulphide reduction. PAF activity was regained by the binding of small factor VIII oligomers to colloidal gold granules with a mean diameter of 23 nm. In contrast, adsorption of large factor VIII polymers onto gold particles resulted in partial loss of PAF activity. Thus, an optimum multimeric size of bovine factor VIII appears to be required for the maximal expression of PAF activity. Gold granules, coated with reduced factor VIII, can be used as an electron-dense label. Their interaction with surface receptors for bovine factor VIII on either viable or formalin-fixed human platelets was demonstrated by transmission and scanning electron microscopy.
血小板聚集因子（PAF）活性优先与较大分子形式的牛因子VIII相关，并且在通过温和的二硫键还原解离成较小的寡聚体后显著降低。通过将小的因子VIII寡聚体与平均直径为23nm的胶体金颗粒结合，PAF活性得以恢复。相比之下，将大的因子VIII聚合物吸附到金颗粒上导致PAF活性部分丧失。因此，牛因子VIII似乎需要最佳的多聚体大小才能最大程度地表达PAF活性。涂有还原型因子VIII的金颗粒可作为电子致密标记物。通过透射电子显微镜和扫描电子显微镜证明了它们与活的或福尔马林固定的人血小板上牛因子VIII的表面受体的相互作用。
