[Qualitative analysis of the binding of fibrin in organic tissue (author's transl)]

The binding energy (EB) of oxygen, sulphur and nitrogen was determined in highly concentrated fibrin, collagen, liver parenchyma and muscle tissue using photoelectron spectrometry. Fibrin was mixed with the collagen, liver or muscle homogenisate, with or without substitution of clotting factor XIII or additional inhibiton of fibrinolysis and the EB was determined again. Changes in the binding energy arise from an alteration in chemical binding. The present investigation showed that fibrin builds up new linkages in liver parenchyma and in collagen using nitrogen bonds and, additionally via a sulphur bond. After addition of fibrin stabilizing factor a new chemical link appeared between fibrin and collagen again through a nitrogen bond and, additionally via a sulphur bond. The inhibition of fibrinolysis produced a new oxygen linkage in all the examined substances (fibrin-tissue).