Some properties of human small heat shock protein Hsp22 (H11 or HspB8)

被引：59

作者：

Kim, MV

Seit-Nebi, AS

Marston, SB

Gusev, NB ^{[1
]}

机构：

[1] Moscow MV Lomonosov State Univ, Sch Biol, Dept Biochem, Moscow 119992, Russia

[2] Univ London Imperial Coll Sci Technol & Med, Sch Med, Natl Heart & Lung Inst, London SW3 6LY, England

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2004年 / 315卷 / 04期

基金：

英国惠康基金; 俄罗斯基础研究基金会;

关键词：

small heat shock proteins; protein kinases; phosphorylation; chaperone activity;

D O I：

10.1016/j.bbrc.2004.01.130

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：796 / 801

页数：6

共 23 条

[1] Increased expression of a novel heat shock protein transcript in the mouse uterus during decidualization and in response to progesterone [J].