EFFECT OF HYPOCHLORITE- AND PEROXIDE-INDUCED OXIDATION OF FIBRINOGEN ON THE FIBRIN STRUCTURE
By applying the methods of dynamic and elastic light scattering and confocal laser scanning microscopy the damage in the spatial fibrin structure during peroxide- and hypochlorite-induced oxidation of fibrinogen has been explored. While peroxide had weak effect on the structural organization of fibrin, the hypochlorite caused the formation of abnormal fibrin with reduced individual fiber diameter coupled with decreased porosity. Measurements of the size distributions of the different samples of fibrinogen revealed a decrease in the hydrodynamic sizes of the oxidized fibrinogen molecules. These results indicate that the hydrophobicity of fibrinogen surface became increased hereupon the oxidized molecules tended to decrease in its colloidal stability. The possible role of oxidative sites in the assembly of structurally abnormal fibrin is analyzes.