Thermal denaturation and aggregation of apoform of glycogen phosphorylase b. Effect of crowding agents and chaperonesстатья

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[1] Thermal denaturation and aggregation of apoform of glycogen phosphorylase b. effect of crowding agents and chaperones / T. B. Eronina, N. A. Chebotareva, S. G. Roman et al. // Biopolymers. — 2014. — Vol. 101, no. 5. — P. 504–516. The effect of protein and chemical chaperones and crowders on thermal stability and aggregation of apoform of rabbit muscle glycogen phosphorylase b (apoPhb) has been studied at 37 grad.C. Proline suppressed heat-induced loss in ability of apoPhb to reconstitution at 37grad.C, whereas a-crystallin did not reveal a protective action. To compare the antiaggregation activity of intact and crosslinked a-crystallins, an adsorption capacity (AC) of a protein chaperone with respect to a target protein was estimated. This parameter is a measure of the antiaggregation activity. Crosslinking of a-crystallin results in 11- fold decrease in the initial AC. The nonlinear character of the relative initial rate of apoPhb aggregation versus the [intact a-crystallin]/[apoPhb] ratio plot is indicative of the decrease in the AC of a-crystallin with increasing the [a-crystallin]/[apoPhb] ratio and can be interpreted as an evidence for dynamic chaperone structure and polydispersity of a-crystallin–target protein complexes. As for chemical chaperones, a semisaturation concentration of the latter was used as a characteristic of the antiaggregation activity. A decrease in the semisaturation concentration for proline was observed in the presence of the crowders (polyethylene glycol and Ficoll-70). VC 2013 Wiley Periodicals, Inc. Biopolymers 101: 504–516, 2014. Keywords: apoform of glycogen phosphorylase b; thermal denaturation; thermal aggregation; protein chaperones; chemical chaperones. [ DOI ]

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