Thermal denaturation and aggregation of apoform of glycogen phosphorylase b. Effect of crowding agents and chaperonesстатья
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Дата последнего поиска статьи во внешних источниках: 23 декабря 2016 г.
Аннотация: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