Weinstein M J, Deykin D
Br J Haematol. 1978 Dec;40(4):617-30. doi: 10.1111/j.1365-2141.1978.tb05838.x.
The molecular weight heterogeneity of fibrinogen from the whole plasma of 12 normal and seven cirrhotic individuals was examined by means of a novel two-dimensional sodium dodecyl suphate (SDS) gel electrophoretic technique. Fibrinogen was first separated from other plasma proteins on a large pore gel, cut out of the gel, reduced, and separated into its component Aalpha, Bbeta and gamma chains on a second gel. Fibrinogen was resolved into two major bands, I and II, on the first gel. The ratio of fibrinogen II to fibrinogens I plus II was approximately 0.3 (range 0.2-0.35) for both normals and cirrhotic patients. Two major molecular weight (mol wt) forms of Aalpha chain were present in normal fibrinogen I: Aalpha/I and/or Aalpha/2, mol wt 7 X 10(4) and 6.7 X 10(4) respectively. Normal fibrinogen II contained either one of these Aalpha chains plus one of the smaller Aalpha chains, Aalpha/6--10, accounting for the 3--4 X 10(4) mol wt difference between bands I and II. Aalpha/2 comprised 33% of the total Aalpha chains (range 27--41%) in normal fibrinogen I and approximately 25% of the Aalpha chains in normal fibrinogen II. In contrast, fibrinogen I from six out of the seven patients contained a lower percentage of Aalpha/2 (range 10--25%). Similarly fibrinogen II from these patients was deficient in Aalpha/2, although the protein contained normal levels of lower mol wt Aalpha derivatives. No correlation was found between per cent fibrinogen II and per cent Aalpha/2 in either normal or cirrhotic subjects. These results suggest that at least two independent processes are responsible for the observed levels of Aalpha heterogeneity in normals and cirrhotics and that the process controlling Aalpha/2 production is a abnormal in cirrhotic individuals. This decrease in Aalpha/2 does not affect the coagulability of fibrinogen. Fibrin monomer aggregation studies indicate that a serum component is, in part, responsible for the abnormally transparent clot formed from the plasma of cirrhotics.
采用一种新型的二维十二烷基硫酸钠（SDS）凝胶电泳技术，检测了12名正常人和7名肝硬化患者全血中纤维蛋白原的分子量异质性。首先在大孔凝胶上从其他血浆蛋白中分离出纤维蛋白原，将凝胶条带切下、还原，然后在第二块凝胶上分离出其组成成分α、β和γ链。在第一块凝胶上，纤维蛋白原可分为两条主要条带，I和II。正常人和肝硬化患者的纤维蛋白原II与纤维蛋白原I加II的比例约为0.3（范围0.2 - 0.35）。正常纤维蛋白原I中存在两种主要分子量形式的α链：α/I和/或α/2，分子量分别为7×10⁴和6.7×10⁴。正常纤维蛋白原II包含这些α链中的一条加上较小的α链之一，α/6 - 10，这解释了条带I和II之间3 - 4×10⁴的分子量差异。α/2在正常纤维蛋白原I的总α链中占33%（范围27 - 41%）,在正常纤维蛋白原II的α链中约占25%。相比之下，7名患者中有6名患者的纤维蛋白原I中α/2的百分比更低（范围10 - 25%）。同样，这些患者的纤维蛋白原II中α/2缺乏，尽管该蛋白中低分子量α衍生物的水平正常。在正常或肝硬化受试者中，未发现纤维蛋白原II百分比与α/2百分比之间存在相关性。这些结果表明，至少有两个独立的过程导致了正常人和肝硬化患者中观察到的α异质性水平，并且控制α/2产生的过程在肝硬化个体中是异常的。α/2的这种减少并不影响纤维蛋白原的凝血性。纤维蛋白单体聚集研究表明，血清成分部分导致了肝硬化患者血浆形成异常透明的凝块。
