Latallo Z S, Mattler L E, Bang N U, Hansen M S, Chang M L
Biochim Biophys Acta. 1976 Jan 20;420(1):69-80. doi: 10.1016/0005-2795(76)90345-7.
The molecular makeup of soluble fibrin complexes was studied by gel exclusion chromatography using radio-labelling to characterize individual components in protein mixtures. Products of limited plasmin degradation of fibrinogen and mixtures of fibrinogen and "early" fibrinogen digests formed high molecular weight soluble fibrin complexes upon incubation with thrombin. Purified, nonclottable fragment Y did not incorporate into soluble fibrin complexes, nor could we demonstrate incorporation of fragments D and E as previously described from our laboratory. Thus, under the conditions of these experiments, soluble fibrin complexes have two identifiable components, fibrin monomer and clottable fragment X monomer, although incorporation of native fibrinogen or fragment X unreacted by thrombin into soluble fibrin complexes cannot be excluded. Individual fractions of thrombin-treated early fibrinogen digests isolated by agarose gel chromatography were treated with protamine sulfate at 37 degrees C resulting in precipitation-gelation of greater than 90 per cent of high molecular weight soluble fibrin complexes; whereas, less than 10 per cent of lower molecular weight fibrinogen degradation products precipitated by protamine sulfate. These findings do not support the widely held concept that soluble fibrin complexes incorporate nonclottable degradation products of fibrinogen proteolysis, nor do they support the notion that the so-called paracoagulation reaction induced by protamine sulfate results from the splitting of complexes between fibrin monomer and nonclottable fibrinogen degradation products.
通过凝胶排阻色谱法研究可溶性纤维蛋白复合物的分子组成，利用放射性标记来表征蛋白质混合物中的各个成分。纤维蛋白原的有限纤溶酶降解产物以及纤维蛋白原与“早期”纤维蛋白原消化物的混合物在与凝血酶孵育后形成高分子量可溶性纤维蛋白复合物。纯化的、不可凝的片段Y未掺入可溶性纤维蛋白复合物中，我们也无法证明如我们实验室先前所述的片段D和E的掺入。因此，在这些实验条件下，可溶性纤维蛋白复合物有两个可识别的成分，纤维蛋白单体和可凝片段X单体，尽管不能排除天然纤维蛋白原或未被凝血酶作用的片段X掺入可溶性纤维蛋白复合物的可能性。通过琼脂糖凝胶色谱法分离的凝血酶处理的早期纤维蛋白原消化物的各个组分在37℃下用硫酸鱼精蛋白处理，导致超过90%的高分子量可溶性纤维蛋白复合物沉淀 - 凝胶化；而硫酸鱼精蛋白沉淀的低分子量纤维蛋白原降解产物不到10%。这些发现不支持广泛持有的可溶性纤维蛋白复合物掺入纤维蛋白原蛋白水解的不可凝降解产物的概念，也不支持硫酸鱼精蛋白诱导的所谓副凝血反应是由纤维蛋白单体与不可凝纤维蛋白原降解产物之间的复合物分裂引起的观点。
