Kanaide H, Uranishi T, Nakamura M
Am J Hematol. 1982 Nov;13(3):229-37. doi: 10.1002/ajh.2830130306.
Effects of divalent cations on fibrinogen and its reaction with thrombin were re-examined and correlated to improve definition of mechanisms underlying the acceleration of clot formation by the ions. The rate of release of fibrinopeptides from fibrinogen was not affected by any of the specific ions studied, but increased rates of fibrin monomer polymerization were obtained with all but magnesium ions. Maximal acceleration of monomer polymerization was observed with the divalent ions at concentration of 2.5-5 mM, and no added specific ion effects were observed with much higher levels. The acceleratory ions were found to have a corresponding effect on the solubility of fibrinogen, as judged from acceleration of its precipitation at low temperature. Although magnesium ions had no effect on fibrin monomer polymerization, they did have a low ranking effect on cryoprecipitation. These data confirm that the principal effect of divalent cations in the fibrinogen-fibrin transformation is to accelerate fibrin monomer polymerization, and suggest that the acceleration is associated with effects on the solubility of fibrinogen.
对二价阳离子对纤维蛋白原及其与凝血酶反应的影响进行了重新研究并建立关联，以完善对离子加速凝血形成机制的定义。从纤维蛋白原释放纤维蛋白肽的速率不受所研究的任何特定离子影响，但除镁离子外，所有离子均使纤维蛋白单体聚合速率增加。在二价离子浓度为2.5 - 5 mM时观察到单体聚合的最大加速，在更高浓度下未观察到添加特定离子的影响。从低温下其沉淀加速判断，加速离子对纤维蛋白原的溶解度有相应影响。尽管镁离子对纤维蛋白单体聚合无影响，但它们对冷沉淀有较低程度的影响。这些数据证实二价阳离子在纤维蛋白原 - 纤维蛋白转化中的主要作用是加速纤维蛋白单体聚合，并表明这种加速与对纤维蛋白原溶解度的影响有关。
