A thermal after-effect of UV irradiation of muscle glycogen phosphorylase b.
basic_science · Level V
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- Record sourced from PubMed, PMID 29216272.
- Also identified by DOI 10.1371/journal.pone.0189125 and PMC identifier 5720721.
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Abstract
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-Phb) 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-Phb molecule, which contains concealed damage.
Medical subject headings
- Glycogen Phosphorylase
- Muscle, Skeletal
- Ultraviolet Rays