Litvinov R I, Zubairov D M
Biokhimiia. 1988 Jul;53(7):1203-13.
The effects of fibronectin on fibrinogen clotting induced by thrombin or reptilase and on fibrin monomer polymerization in a pure system in the absence of factor XIIIa were studied. It was shown that within a broad range of concentrations and molar ratios of the mixed proteins, fibronectin does not alter significantly the fibrinogen clotting time either under thrombin or under reptilase action. The effect of fibronectin on the fibrin self-assembly consists in a slight acceleration of this process, whose degree is directly dependent on the fibronectin/fibrin monomer molar ratio as well as on the absolute fibrin monomer content at a constant molar ratio. The stimulating effect of fibronectin is amplified by Ca2+. The experimental results suggest that fibronectin can noncovalently bind the fibrin monomer and/or intermediate polymers in the non-enzymatic phase of fibrinogen conversion to fibrin.
研究了纤连蛋白对凝血酶或蛇毒凝血酶诱导的纤维蛋白原凝血以及在无因子XIIIa的纯体系中对纤维蛋白单体聚合的影响。结果表明,在混合蛋白的广泛浓度和摩尔比范围内,纤连蛋白在凝血酶或蛇毒凝血酶作用下均不会显著改变纤维蛋白原的凝血时间。纤连蛋白对纤维蛋白自组装的影响在于轻微加速这一过程,其程度直接取决于纤连蛋白/纤维蛋白单体摩尔比以及在恒定摩尔比下的绝对纤维蛋白单体含量。Ca2+可增强纤连蛋白的刺激作用。实验结果表明,在纤维蛋白原转化为纤维蛋白的非酶促阶段,纤连蛋白可与纤维蛋白单体和/或中间聚合物非共价结合。