Abstract:
: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°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°C n=2 and the rate-limiting stage is aggregation of unfolded protein molecules.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Eronina TB,Mikhaylova VV,Chebotareva NA,Kurganov BIdoi
10.1016/j.ijbiomac.2016.08.038subject
Has Abstractpub_date
2016-11-01 00:00:00pages
1252-1257eissn
0141-8130issn
1879-0003pii
S0141-8130(16)31193-Xjournal_volume
92pub_type
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