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Some properties of human small heat shock protein Hsp22 (H11 or HspB8).
2004 (English)In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 315, no 4Article in journal (Refereed) Published
Abstract [en]

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 20 kDa (Hsp20).

Place, publisher, year, edition, pages
2004. Vol. 315, no 4
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Natural Sciences Biochemistry and Molecular Biology
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URN: urn:nbn:se:umu:diva-128274DOI: 10.1016/j.bbrc.2004.01.130PubMedID: 14985082OAI: oai:DiVA.org:umu-128274DiVA, id: diva2:1051096
Available from: 2016-12-01 Created: 2016-12-01 Last updated: 2018-06-09

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Kim, Maria V

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