A thermal after-effect of UV irradiation of muscle glycogen phosphorylase b | Zendy

Valeriya V. Mikhaylova | Zendy; Tatiana B. Eronina | Zendy; Natalia A. Chebotareva | Zendy; Sergey Y. Kleymenov | Zendy; Vladimir V. Shubin | Zendy; Boris I. Kurganov | Zendy

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A thermal after-effect of UV irradiation of muscle glycogen phosphorylase b

Author(s) -

Valeriya V. Mikhaylova,

Tatiana B. Eronina,

Natalia A. Chebotareva,

Sergey Y. Kleymenov,

Vladimir V. Shubin,

Boris I. Kurganov

Publication year - 2017

Publication title -

plos one

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.99

H-Index - 332

ISSN - 1932-6203

DOI - 10.1371/journal.pone.0189125

Subject(s) - glycogen phosphorylase , glycogen , biophysics , irradiation , chemistry , protein aggregation , kinetics , chaperone (clinical) , biochemistry , limiting , protein folding , biology , medicine , mechanical engineering , physics , pathology , quantum mechanics , nuclear physics , engineering

Different test systems are used to characterize the anti-aggregation efficiency of molecular chaperone proteins and of low-molecular-weight chemical chaperones. Test systems based on aggregation of UV-irradiated protein are of special interest because they allow studying the protective action of different agents at physiological temperatures. The kinetics of UV-irradiated glycogen phosphorylase b (UV-Ph b ) from rabbit skeletal muscle was studied at 37°C using dynamic light scattering in a wide range of protein concentrations. It has been shown that the order of aggregation with respect to the protein is equal to unity. A conclusion has been made that the rate-limiting stage of the overall process of aggregation is heat-induced structural reorganization of a UV-Ph b molecule, which contains concealed damage.

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