Cornelius R M, Brash J L
Department of Chemical Engineering, McMaster University, Hamilton, Ontario, Canada.
J Biomed Mater Res. 1997 Dec 5;37(3):314-23. doi: 10.1002/(sici)1097-4636(19971205)37:3<314::aid-jbm2>3.0.co;2-o.
The adsorption of fibrinogen from a single protein solution and from binary mixtures of fibrinogen and high-molecular-weight kininogen (HK) to glass and four sulfonated polyurethane surfaces is reported. The effect of the single-chain (SCHK) and two-chain (TCHK) forms of HK on fibrinogen adsorption was investigated. Using radiolabeling methods, fibrinogen adsorption from a series of mixtures having the same weight ratio of fibrinogen to HK as in plasma (50:1), but varying in total concentration, was measured. Fibrinogen adsorption from the mixtures was reduced on all surfaces compared to the single-protein solution, confirming the highly surface-active nature of this protein. However, except for glass, there was no significant difference between the SCHK and TCHK forms. Polyacrylamide gel electrophoresis and immunoblotting analysis of the proteins eluted from the surfaces after contact with the fibrinogen-SCHK solutions indicated that although intact SCHK was essentially conserved, some transformation of SCHK to TCHK on the surface occurred during the course of the experiment. It is hypothesized that in purified form, in which HK is not complexed to prekallikrein or factor XI, the surface-binding domain is more available than in the complexed forms which are present in plasma. If so, then the removal of bradykinin by kallikrein, as occurs in generating TCHK, may not be required for the expression of surface-binding domain activity.
本文报道了纤维蛋白原从单一蛋白质溶液以及从纤维蛋白原与高分子量激肽原（HK）的二元混合物中吸附到玻璃和四种磺化聚氨酯表面的情况。研究了HK的单链形式（SCHK）和双链形式（TCHK）对纤维蛋白原吸附的影响。采用放射性标记方法，测定了一系列具有与血浆中相同纤维蛋白原与HK重量比（50:1）但总浓度不同的混合物中纤维蛋白原的吸附情况。与单一蛋白质溶液相比，混合物中纤维蛋白原在所有表面的吸附均减少，这证实了该蛋白质具有高度的表面活性。然而，除玻璃外，SCHK和TCHK形式之间没有显著差异。对与纤维蛋白原 - SCHK溶液接触后从表面洗脱的蛋白质进行聚丙烯酰胺凝胶电泳和免疫印迹分析表明，尽管完整的SCHK基本保持不变，但在实验过程中表面上发生了一些SCHK向TCHK的转化。据推测，在纯化形式中，HK未与前激肽释放酶或因子XI结合，其表面结合结构域比血浆中存在的复合形式更易获得。如果是这样，那么在产生TCHK时激肽释放酶对缓激肽的去除可能不是表面结合结构域活性表达所必需的。
