Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10770538 | Biochemical and Biophysical Research Communications | 2005 | 6 Pages |
Abstract
Effect of recombinant chicken small heat shock protein with molecular mass 24Â kDa (Hsp24) and recombinant human small heat shock protein with molecular mass 27Â 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.
Keywords
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Anastasiya V. Pivovarova, Valeria V. Mikhailova, Ivan S. Chernik, Natalia A. Chebotareva, Dmitrii I. Levitsky, Nikolai B. Gusev,