Journal
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 92, Issue -, Pages 1252-1257Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.ijbiomac.2016.08.038
Keywords
Glycogen phosphorylase b; Holo- and apoforms; Thermal aggregation; Kinetic regime
Funding
- Russian Foundation for Basic Research [16-04-00560-a, 14-04-01530-a]
- Program Molecular and Cell Biology of the Presidium of the Russian Academy of Sciences
- Russian Science Foundation [16-14-10055]
- Russian Science Foundation [16-14-10055] Funding Source: Russian Science Foundation
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To characterize the role of pyridoxal 5'-phosphate in stabilization of the conformation of muscle glycogen phosphorylase b (Phb), the mechanism of thermal aggregation for holo- and apoforms of Phb has been studied using dynamic light scattering. The order of aggregation with respect to the protein (n) for aggregation of holoPhb at 48 degrees C is equal to 0.5 suggesting that the dissociative mechanism of denaturation is operative and denaturation is followed by rapid aggregation stage. In the case of aggregation of apoPhb at 37 degrees C n=2 and the rate-limiting stage is aggregation of unfolded protein molecules. (C) 2016 Elsevier B.V. All rights reserved.
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