Journal
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 118, Issue -, Pages 1193-1202Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.ijbiomac.2018.06.185
Keywords
UV-irradiated muscle glycogen phosphorylase b; Thermal aggregation; Ionic strength; Arginine
Funding
- Russian Science Foundation [16-14-10055]
- Federal Agency of Scientific Organizations [0104-2018-0009]
- Russian Science Foundation [16-14-10055] Funding Source: Russian Science Foundation
Ask authors/readers for more resources
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 degrees 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 k(1). It was shown that an increase in NaCl concentration caused a decrease in the k(1) 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, experiments were conducted at fixed values of ionic strength (0.15 M and 0.5 M). It was shown that at a low ionic 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. (C) 2018 Elsevier B.V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available