Effects of small heat shock proteins on the thermal denaturation and aggregation of F-actin
| Autor: | Nikolai B. Gusev, Natalia A. Chebotareva, Ivan S. Chernik, Dmitrii I. Levitsky, Valeria V. Mikhailova, Anastasiya V. Pivovarova |
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| Rok vydání: | 2005 |
| Předmět: |
Protein Denaturation
Biophysics macromolecular substances Biochemistry law.invention Differential scanning calorimetry Hsp27 law Heat shock protein Animals Humans Denaturation (biochemistry) Cytoskeleton Molecular Biology Heat-Shock Proteins Actin Calorimetry Differential Scanning Molecular mass biology Chemistry Cell Biology Actins Recombinant DNA biology.protein Chickens |
| Zdroj: | Biochemical and Biophysical Research Communications. 331:1548-1553 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/j.bbrc.2005.04.077 |
| Popis: | Effect of recombinant chicken small heat shock protein with molecular mass 24 kDa (Hsp24) and recombinant human small heat shock protein with molecular mass 27 kDa (Hsp27) on the heat-induced denaturation and aggregation of skeletal F-actin was analyzed by means of differential scanning calorimetry and light scattering. All small heat shock proteins did not affect thermal unfolding of F-actin measured by differential scanning calorimetry, but effectively prevented aggregation of thermally denatured actin. Small heat shock protein formed stable complexes with denatured (but not with intact) F-actin. The size of these highly soluble complexes was smaller than the size of intact F-actin filaments. It is supposed that protective effect of small heat shock proteins on the cytoskeleton is at least partly due to prevention of aggregation of denatured actin. |
| Databáze: | OpenAIRE |
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