Mechanism of the action of factor XIII on the structure of fibrin in the normal and pathological states.
The work discusses the influence of factor XIII on the molecular structure of fibrin and its properties under normal conditions and in certain forms of coagulopathies. It was shown that the reaction of stabilization is accompanied by an exothermic effect, the thermal effect of which on donor blood plasma is 15.5 kcal/mole. It was also established that the enrichment of blood plasma with fibrinogen leads to an increase in the thermal effect, which is due to the influence of the density of the terminal and lateral bonds in the fibrin molecule and the process of its covalent cross-linking. An examination of groups of patients structure of fibrin and its physiological properties, on account of a change in the number of peptide bonds formed. On the basis of the results obtained, a new energy test for the determination of the fibrin-stabilizing factor is suggested.
D001778:Blood Coagulation Disorders / Q000378:metabolism*; D005176:Factor XIII / Q000378:metabolism*; D005337:Fibrin / Q000378:metabolism*; D006358:Hot Temperature; D006801:Humans; D010455:Peptides / Q000378:metabolism; D011485:Protein Binding; D013816:Thermodynamics
D010455:Peptides; D005337:Fibrin; D005176:Factor XIII