Kinetic regime of thermal aggregation of holo- and apoglycogen phosphorylases b.

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 Macromol

authors

Eronina TB,Mikhaylova VV,Chebotareva NA,Kurganov BI

doi

10.1016/j.ijbiomac.2016.08.038

subject

Has Abstract

pub_date

2016-11-01 00:00:00

pages

1252-1257

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(16)31193-X

journal_volume

92

pub_type

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