Comparative analysis of the influence of chlorine and fluorine anions on the fibrin polymerization
| Autor: | L. V. Pyrogova, G. K. Bereznitsky, G. K. Gogolinskaya, T. M. Platonova, I. M. Kolesnikova, O. O. Masenko, R. Yu. Marunich, P. Yu. Tsap, Yu. V. Ushenin, Y. M. Makogonenko, E. V. Lugovskoi |
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| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: | |
| Zdroj: | The Ukrainian Biochemical Journal, Vol 91, Iss 6, Pp 27-37 (2019) |
| Druh dokumentu: | article |
| ISSN: | 2409-4943 2413-5003 |
| DOI: | 10.15407/ubj91.06.027 |
| Popis: | The effect of NaCl and NaF salts in the range of 0.1-0.225 M concentrations on individual stages of fibrin polymerization was investigated, namely: the rate of fibrinogen activation by thrombin, the rate of protofibrils formation, the rate of lateral association of protofibrils, and the maximum clot absorbance value at 350 nm. It was found that the chlorine and fluorine anions equally inhibit the rate of formation of fibrin from fibrinogen and the formation of protofibrils activated with thrombin. Chlorine anions were shown to be significantly more effective than fluorine anions, inhibiting the rate of lateral association and maximal clot absorbance level from fibrin desA and desAB. A component of the inhibitory action of chlorine anions, not related to the ionic strength of the solution, was identified and its effect on the individual polymerization steps was shown. Chlorine anions were found to bind to a fibrin clot. Using the surface plasmon resonance method and fibrin-specific mAb FnI-3c, it was established that the rate of exposure of neoantigenic determinants of mAb in the hinge regions of the fibrinogen molecule during its transformation into fibrin under the action of thrombin is inhibited by chlorine anions in correlation with inhibition of the protofibril lateral association rate. It has been suggested that the inhibitory effect of chlorine anions consists of an ionic component and a component that blocks the conformational mobility of the molecule by the chlorine anions binding to its hinge regions and polymerization sites. |
| Databáze: | Directory of Open Access Journals |
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