期刊
BIOPOLYMERS
卷 101, 期 5, 页码 504-516出版社
WILEY
DOI: 10.1002/bip.22410
关键词
apoform of glycogen phosphorylase b; thermal denaturation; thermal aggregation; protein chaperones; chemical chaperones
资金
- Russian Foundation for Basic Research [11-04-01271-a, 11-04-00932-a]
- Presidium of the Russian Academy of Sciences (Program Molecular and Cell Biology)
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 degrees C. Proline suppressed heat-induced loss in ability of apoPhb to reconstitution at 37 degrees C, whereas -crystallin did not reveal a protective action. To compare the antiaggregation activity of intact and crosslinked -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 -crystallin results in 11-fold decrease in the initial AC. The nonlinear character of the relative initial rate of apoPhb aggregation versus the [intact -crystallin]/[apoPhb] ratio plot is indicative of the decrease in the AC of -crystallin with increasing the [-crystallin]/[apoPhb] ratio and can be interpreted as an evidence for dynamic chaperone structure and polydispersity of -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). (c) 2013 Wiley Periodicals, Inc. Biopolymers 101: 504-516, 2014.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据