Fass D N, Knutson G J, Bowie E J
J Lab Clin Med. 1978 Feb;91(2):307-20.
Purified porcine Willebrand factor was analyzed by agarose-sodium DodSO4 electrophoresis. Multiple forms of the protein were found in a series of increasing molecular weights. A molecular mass calibration curve was constructed with fibrinogen (3.4 X 10(5) daltons), IgM (1 X 10(6) daltons), and glutaraldehyde-crosslinked IgM polymers (2, 3, and 4 X 10(6) daltons). As measured by this procedure, the apparent molecular weight of Willebrand factor polymers ranged from 1.1 X 10(6) to 2.1 X 10(7). Each member of the series differed from one another by approximately 1.5 to 1.9 X 10(6) daltons, indicating that members of the series were polymers of 6-mers to 8-mers of the 2.3 X 10(5) dalton subunit. Various purification procedures, used to isolate Willebrand factor active in inducing platelet aggregation, were seen to fractionate the polymers, in part, on the basis of size. The same purification procedures, when applied to procine von Willebrand plasma, failed to yield protein of molecular weight greater than 1.1 X 10(6).
采用琼脂糖 - 十二烷基硫酸钠电泳法对纯化的猪血管性血友病因子进行分析。在一系列分子量逐渐增加的情况下发现了该蛋白质的多种形式。用纤维蛋白原（3.4×10⁵道尔顿）、免疫球蛋白M（1×10⁶道尔顿）和戊二醛交联的免疫球蛋白M聚合物（2×10⁶、3×10⁶和4×10⁶道尔顿）构建了分子量校准曲线。通过该方法测量，血管性血友病因子聚合物的表观分子量范围为1.1×10⁶至2.1×10⁷。该系列的每个成员彼此相差约1.5至1.9×10⁶道尔顿，表明该系列成员是由2.3×10⁵道尔顿亚基的6聚体至8聚体组成的聚合物。用于分离具有诱导血小板聚集活性的血管性血友病因子的各种纯化程序，部分是根据大小对聚合物进行分级分离。当将相同的纯化程序应用于猪血管性血友病血浆时，未能得到分子量大于1.1×10⁶的蛋白质。
