Reversible Dimerization of Human Serum Albumin Научная публикация
Журнал |
Molecules
, E-ISSN: 1420-3049 |
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Вых. Данные | Год: 2021, Том: 26, Номер: 1, Номер статьи : 108, Страниц : DOI: 10.3390/molecules26010108 | ||||||||||
Ключевые слова | human serum albumin; pulse dipole EPR; aggregation | ||||||||||
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Реферат:
Pulsed Dipolar Spectroscopy (PDS) methods of Electron Paramagnetic Resonance (EPR) were used to detect and characterize reversible non-covalent dimers of Human Serum Albumin (HSA), the most abundant protein in human plasma. The spin labels, MTSL and OX063, were attached to Cys-34 and these chemical modifications of Cys-34 did affect the dimerization of HSA, indicating that other post-translational modifications can modulate dimer formation. At physiologically relevant concentrations, HSA does form weak, non-covalent dimers with a well-defined structure. Dimer formation is readily reversible into monomers. Dimerization is very relevant to the role of HSA in the transport, binding, and other physiological processes.
Библиографическая ссылка:
Chubarov A.
, Spitsyna A.
, Krumkacheva O.
, Mitin D.
, Suvorov D.
, Tormyshev V.
, Fedin M.
, Bowman M.K.
, Bagryanskaya E.
Reversible Dimerization of Human Serum Albumin
Molecules. 2021. V.26. N1. 108 . DOI: 10.3390/molecules26010108 WOS Scopus
Reversible Dimerization of Human Serum Albumin
Molecules. 2021. V.26. N1. 108 . DOI: 10.3390/molecules26010108 WOS Scopus
Файлы:
Полный текст от издателя
Даты:
Опубликована online: | 29 дек. 2020 г. |
Идентификаторы:
Web of science | WOS:000606042300001 |
Scopus | 2-s2.0-85099176329 |
OpenAlex | W3117876055 |