Hopmeier P, Halbmayer M, Fischer M, Marx G
Central Laboratory, Krankenhaus Wien-Lainz, Vienna, Austria.
Thromb Res. 1990 May 1;58(3):293-301. doi: 10.1016/0049-3848(90)90099-x.
Human thrombin with high affinity to Sepharose insolubilized fibrin monomers (high-affinity thrombin) was used to investigate the effect of Zn(II) on the thrombin adsorption to fibrin. Results showed that at Zn(II) concentrations exceeding 100 mumols/l, thrombin binding to fibrin was decreased concomitant with the Zn(II) concentration and time; at lower Zn(II) concentrations, thrombin adsorption was enhanced. Experimental results were identical by using 125I-labelled high-affinity alpha-thrombin or by measuring the thrombin activity either by chromogenic substrate or by a clotting time method. In contrast, Ca(II) alone (final conc. 3 mmol/l) or in combination with Zn(II) was not effective. However, at higher Ca(II) concentrations (7.5-15 mmol/l), thrombin adsorption was apparently decreased. Control experiments revealed that Zn(II) had no impact on the clottability of fibrinogen, and that the results of the experiments with Ca(II) were not altered by possible cross-linking of fibrin. We conclude that unlike Ca(II), Zn(II) is highly effective in modulating thrombin adsorption to fibrin.
使用对固定在琼脂糖上的纤维蛋白单体具有高亲和力的人凝血酶（高亲和力凝血酶）来研究锌离子（Zn(II)）对凝血酶吸附到纤维蛋白上的影响。结果表明，当Zn(II)浓度超过100微摩尔/升时，凝血酶与纤维蛋白的结合随Zn(II)浓度和时间的增加而减少；在较低的Zn(II)浓度下，凝血酶的吸附增强。使用125I标记的高亲和力α-凝血酶，或者通过发色底物法或凝血时间法测量凝血酶活性，实验结果是相同的。相比之下，单独的钙离子（Ca(II)，终浓度3毫摩尔/升）或与Zn(II)联合使用均无效。然而，在较高的Ca(II)浓度（7.5 - 15毫摩尔/升）下，凝血酶的吸附明显减少。对照实验表明，Zn(II)对纤维蛋白原的凝血能力没有影响，并且Ca(II)实验的结果不会因纤维蛋白可能的交联而改变。我们得出结论，与Ca(II)不同，Zn(II)在调节凝血酶对纤维蛋白的吸附方面非常有效。
