| Autor: |
I.V. Gorudko, D.V. Grigorieva, E.V. Shamova, N.P. Gorbunov, A.U. Kokhan, V.A. Kostevich, V.B. Vasilyev, O.M. Panasenko, N.V. Khinevich, H.V. Bandarenka, A.A. Burko, A.V. Sokolov |
| Rok vydání: |
2022 |
| Předmět: |
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| Zdroj: |
Archives of biochemistry and biophysics. 728 |
| ISSN: |
1096-0384 |
| Popis: |
Myeloperoxidase (MPO), an oxidant-producing enzyme of neutrophils, has been shown to prime platelet activity promoting immunothrombosis. Native MPO is a homodimer, consisting of two identical protomers (monomer) connected by a single disulfide bond. But in inflammatory foci, MPO can be found both in the form of a monomer and in the form of a dimer. Beside MPO can also be in complexes with other molecules and be modified by oxidants, which ultimately affect its physicochemical properties and functions. Here we compared the effects of various forms of MPO as well as MPO in complex with ceruloplasmin (CP), a physiological inhibitor of MPO, on the platelet activity. Monomeric MPO (hemi-MPO) was obtained by treating the dimeric MPO by reductive alkylation. MPO was modified with HOCl in a molar ratio of 1:100 (MPO-HOCl). Using surface-enhanced Raman scattering (SERS) spectroscopy we showed that peaks at about 510 and 526 cm |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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