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Effect of ionic strength and arginine on aggregation of UV-irradiated muscle glycogenphosphorylase bTatiana B. Eronina, Valeriya V. Mikhaylova, Natalia A. Chebotareva, Vladimir V. Shubin, Boris I.Kurganovстатья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 8 декабря 2019 г.
- Авторы: Eronina Tatiana B., Mikhaylova Valeriya V., Chebotareva Natalia A., Shubin Vladimir V., Kurganov Boris I.
- Журнал: International Journal of Biological Macromolecules
- Номер: 118
- Год издания: 2018
- Издательство: Elsevier BV
- Местоположение издательства: Netherlands
- Первая страница: 1193
- Последняя страница: 1202
- DOI: 10.1016/j.ijbiomac.2018.06.185
- Аннотация: In this work the effect of ionic strength and arginine on the kinetics of aggregation of UV-irradiated muscle glycogen phosphorylase b (UV-Phb) was studied using dynamic light scattering at 37 °C at various ionic strengths (0.02–0.7 M). Under these conditions the rate-limiting stage of the overall aggregation process is the structural reorganization of UV-Phb, which can be characterized by the first order rate constant kI. It was shown that anincrease in NaCl concentration caused a decrease in the kI value, suggesting a slowdown of the UV-Phb structural reorganization. Circular dichroism data confirmed this conclusion. Arginine is widely used in biotechnology as an agent suppressing protein aggregation. However, arginine is a charged molecule, and, when studying the action of arginine on protein aggregation, the effects of ionic strength should be taken into account. To evaluate the effect of arginine, experimentswere conducted at fixed values of ionic strength (0.15Mand 0.5M). Itwas shown that at a lowionic strength arginine (0–0.13 M) accelerated the process of protein aggregation,whereas at higher ionic strength arginine (0–0.48 M) acted as an aggregation suppressor.
- Добавил в систему: Чеботарева Наталья Александровна