Abstract
The use of two-dimensional electrophoresis to study the polypeptide composition of heat shock proteins 70 synthesized in the myocardium of Wistar and August rats in response to thermal stress and repetitive immobilization stress revealed interstrain differences in the composition of stimulated polypeptides in these proteins. The differences are mainly due to differential expression of the heat shock protein gene(s) encoding polypeptides with pI 6.2–6.0 in the two strains. The drastically reduced levels of the synthesis and/or accumulation of some heat shock proteins 70 in the hearts of August rats are associated with their failure to develop cardioprotective phenomena in response to repetitive immobilization stress.
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