Kinetic regime of thermal aggregation of holo- and apoglycogen phosphorylases bстатья
Статья опубликована в высокорейтинговом журнале
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Дата последнего поиска статьи во внешних источниках: 15 декабря 2016 г.
Аннотация: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.