Abstract
SINCE Hageman factor (HF) was found to participate in fibrinolytic activity1,2 several investigations have been carried out to explore its role in fibrinolysis. Iatridis and Ferguson3, in a detailed analysis of this phenomenon, suggested that Hageman factor has a lysokinase activity which converts plasminogen-proplasminoplastin (proactivator) into plasminoplastin (activator). Aznar et al.4 investigated the fibrinolytic activity of Hageman factor by means of thrombelastography and concluded that the active form itself has a similar character to that of the plasmatic proactivator. Haanen et al.5 showed that the fibrinolytic activity of a purified Hageman factor is only measurable in the presence of plasminogen, and therefore Hageman factor is an activator of plasminogen. But Iatridis and Ferguson3 had shown that chicken plasma, which is deficient in proplasminoplastin (proactivator) and in Hageman factor, did not develop any plasminoplastin (activator) activity, despite the addition of streptokinase or kaolin-SF (surface factor or activation product). Thus, from this experiment and from others using normal or Hageman deficient plasmas, they concluded that activated Hageman factor is only efficient for the generation of endogenous plasminoplastin when its precursor (the proplasminoplastin) is available.
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IATRIDIS, P., FERGUSON, J. Plasminoplastin Generation Test− of Normal, HF−, PTA−, X−, PTC− and AHF− Platelet-poor Plasmas: Evidence that only HF− Plasma has an Abnormal Fibrinolytic Activity. Nature 207, 1404–1405 (1965). https://doi.org/10.1038/2071404a0
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DOI: https://doi.org/10.1038/2071404a0
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