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Severely burned children often show a dysfunction of microcirculation, due to overproduction of O2 radicals and to the activation of blood coagulation. We studied the effect of H2O2 on fibrinogen collected from burned children. Controls were healthy adult donors. Fibrinogen was purified through precipitation with PEG and saltin-out procedure. The thrombin-induced transformation of fibrinogen to fibrin, as assayed by recording the polymerization curves, was faster in the patient native fibrinogen than in controls(n=18, p<0.001). The oxidation of control fibrinogen with H2O2 caused a decrease of the structurally reactive protein (measured by a nephelometric method)and increased the velocity of fibrinogen-fibrin transformation. It was also associated to a decrease of thryptophane residues, as assayed by the spectral changes at 282 nm. At the same experimental conditions, similar changes were not observed in patient fibrinogen. Patient fibrinogen showed a decreased number of aminoacid residues reactive to the “in vitro” oxidation. Our data demonstrate the existence of some structural differences between patient and normal fibrinogen, that may be relevant in the pathophysiologic events following burns.

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Principe, D., Menichelli, A., Giordani, M. et al. DYSFIBRINOGENEMIA IN BURNED CHILDREN. Pediatr Res 26, 504 (1989).

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