Some properties of human small heat shock protein Hsp22 (H11 or HspB8)
Some properties of human small heat shock protein Hsp22 (H11 or HspB8)
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DOI：
10.1016/j.bbrc.2004.01.130
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发表时间：
2004-03-19
影响因子：
3.1
通讯作者：
Gusev, NB
中科院分区：
文献类型：
--
作者：
Kim, MV;Seit-Nebi, AS;Gusev, NB
在均相状态下获得了表观分子量为22 kDa的未标记的重组人小分子热休克蛋白（Hsp 22）。尺寸排阻色谱和与二甲基辛二酰亚胺的化学交联表明Hsp22形成稳定的二聚体。由于对氧化高度敏感，Hsp22形成二硫化物交联的二聚体和难溶的高分子量寡聚体。根据CD光谱，Hsp22的氧化导致二级和三级结构的干扰。Hsp22具有可忽略的低自磷酸化活性，并且在所使用的条件下不能磷酸化酪蛋白或组蛋白。热休克蛋白22能有效地阻止酵母醇脱氢酶和牛肝罗丹酸酶的热诱导聚集，其分子伴侣活性与表观分子量为20kDa的重组人小分子热休克蛋白（Hsp20）相当。(C)2004年爱思唯尔公司All rights reserved.
Untagged recombinant human small heat shock protein with apparent molecular mass 22 kDa (Hsp22) was obtained in homogeneous state. Size exclusion chromatography and chemical crosslinking with dimethylsuberimidate indicate that Hsp22 forms stable dimers. Being highly susceptible to oxidation Hsp22 forms disulfide crosslinked dimers and poorly soluble high molecular mass oligomers. According to CD spectroscopy oxidation of Hsp22 results in disturbing of both secondary and tertiary structure. Hsp22 possesses a negligibly low autophosphorylation activity and under the conditions used is unable to phosphorylate casein or histone. Hsp22 effectively prevents heat-induced aggregation of yeast alcohol dehydrogenase and bovine liver rhodanese with chaperone activity comparable to that of recombinant human small heat shock protein with apparent molecular mass 20kDa (Hsp20). (C) 2004 Elsevier Inc. All rights reserved.