Brezniak D V, Moon D G, Beaver J A, Fenton J W
New York State Department of Health, Wadsworth Center for Laboratories and Research, Albany 12201.
Blood Coagul Fibrinolysis. 1994 Feb;5(1):139-43. doi: 10.1097/00001721-199402000-00016.
Clotting of human plasma by human alpha-thrombin was prolonged in the presence of haemoglobin as was human and bovine fibrinogen. Specifically, the clot time doubled for human plasma, human fibrinogen and bovine fibrinogen at 483, 233, and 116 microM haemoglobin, respectively. Fibrinopeptide A release was not inhibited at concentrations in approximately 16,000 molar excess compared with alpha-thrombin. Turbidometric analysis of fibrin polymerization showed a lengthening of the lag phase as well as the fibrin assembly process in the presence of haemoglobin. These findings suggested that neither fibrinogen recognition nor catalytic efficiency of thrombin was affected, implying that haemoglobin interferes with fibrin polymerization. Since human blood contains sufficient haemoglobin in erythrocytes to generate concentrations of up to 2.3 mM upon cell lysis, and haemoglobin concentrations of 0.16-0.48 mM caused 1.25 to two times longer clotting times in fresh human plasma, respectively, haemoglobin may act to modulate clot formation under conditions of haemolysis.
在血红蛋白存在的情况下，人α-凝血酶对人血浆的凝血作用延长，人纤维蛋白原和牛纤维蛋白原也是如此。具体而言，在血红蛋白浓度分别为483、233和116微摩尔时，人血浆、人纤维蛋白原和牛纤维蛋白原的凝血时间分别增加了一倍。与α-凝血酶相比，在大约16,000摩尔过量的浓度下，纤维蛋白肽A的释放并未受到抑制。对纤维蛋白聚合的比浊分析表明，在血红蛋白存在的情况下，延迟期以及纤维蛋白组装过程都延长了。这些发现表明，纤维蛋白原的识别和凝血酶的催化效率均未受到影响，这意味着血红蛋白会干扰纤维蛋白的聚合。由于人血液中的红细胞含有足够的血红蛋白，细胞裂解后可产生高达2.3毫摩尔的浓度，并且血红蛋白浓度为0.16 - 0.48毫摩尔时，分别使新鲜人血浆中的凝血时间延长了1.25至两倍，因此血红蛋白可能在溶血条件下起调节凝血形成的作用。
