Furlan M, Perret B A, Beck E A
Schweiz Med Wochenschr. 1980 Oct 4;110(40):1456-8.
High molecular weight factor VIII was partially reduced with beta-mercaptoethanol. Disulfide reduction resulted in progressive dissociation of the multimeric protein with a concomitant decrease in von Willebrand activity. The binding of reduced small factor VIII oligomers to gold particles with an average diameter of 20--25 nm led to marked "activation" of their von Willebrand activity. A similar increase in activity was also observed following adsorption of native small molecular weight forms of factor VIII to gold granules. Binding of initially highly active high molecular weight factor VIII to gold granules resulted in inhibition of von Willebrand activity, probably by formation of superaggregates. The platelet aggregating function of factor VIII in the circulation appears to depend largely on the size of this multimeric protein, which must be in the range of several millions for its maximum expression.
高分子量凝血因子VIII被β-巯基乙醇部分还原。二硫键的还原导致多聚体蛋白逐渐解离，同时血管性血友病因子活性降低。还原后的小分子量凝血因子VIII寡聚体与平均直径为20 - 25 nm的金颗粒结合，导致其血管性血友病因子活性显著“激活”。将天然小分子量形式的凝血因子VIII吸附到金颗粒上后，也观察到类似的活性增加。最初高活性的高分子量凝血因子VIII与金颗粒结合导致血管性血友病因子活性受到抑制，这可能是由于形成了超聚集体。循环中凝血因子VIII的血小板聚集功能似乎很大程度上取决于这种多聚体蛋白的大小，其最大表达时大小必须在数百万范围内。
