Hypochlorite-Induced Disturbance in the Secondary Structure of the Coagulation Factor XIII
| Autor: | A. D. Vasilyeva, Alexander N. Shchegolikhin, M. A. Rosenfeld, L. V. Yurina |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
010304 chemical physics
medicine.medical_treatment Hypochlorite chemistry.chemical_element Calcium 010402 general chemistry 01 natural sciences 0104 chemical sciences Catalysis chemistry.chemical_compound Thrombin chemistry Coagulation 0103 physical sciences Fibrinolysis Oxidizing agent medicine Biophysics Physical and Theoretical Chemistry Protein secondary structure medicine.drug |
| Zdroj: | Russian Journal of Physical Chemistry B. 15:123-130 |
| ISSN: | 1990-7923 1990-7931 |
| DOI: | 10.1134/s1990793121010279 |
| Popis: | Coagulation factor XIII (FXII), which is converted into the active form of FXIIIa under the combined action of thrombin and calcium ions, plays an important role in the processes of coagulation and fibrinolysis. It is shown that FXIII, treated with 150 μM hypochlorite, almost completely retains its transglutaminase activity, while in the case of FXIIIa treated with 50 μM hypochlorite, the in the latter it sharply decreases. According to the FTIR spectroscopy data, the action of 150 μM hypochlorite on FXIII, on FXIII partially activated by Ca2+, and on FXIIIa lead to mild violations of the secondary structure of the protein, which are accompanied by a slight decrease in the content of α-helices with an increase in the content of the β-structures. The most noticeable decrease in the content of α-helices is found during the oxidation of FXIIIa. Taking into account the structural features of the catalytic, FXIII-A, and regulatory, FXIII-B, subunits, it seems reasonable to assume that the decrease in the number of α-helices under the action of an oxidizing agent should be due to the structural rearrangements in the domain of the catalytic core. The results of the study indicate that the structure of FXIII is highly resistant to oxidant attack. |
| Databáze: | OpenAIRE |
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