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. 1995 Jan 1;305(Pt 1):197–203. doi: 10.1042/bj3050197

Chemical modifications of a recombinant bovine stress-inducible 70 kDa heat-shock protein (Hsp70) mimics Hsp70 isoforms from tissues.

J A Gutierrez 1, V Guerriero Jr 1
PMCID: PMC1136449  PMID: 7826329

Abstract

A cDNA clone for the stress-inducible 70 kDa heat-shock protein (Hsp70) has been isolated from a bovine skeletal-muscle cDNA library. This mRNA encodes a protein with a calculated molecular mass of 70250 Da. The cDNA has one continuous open reading frame capable of encoding a 641-amino-acid protein. Expression of this cDNA in a bacterial expression system produced a protein with a mobility identical with that of the inducible Hsp70 protein from bovine skeletal muscle as determined by SDS/PAGE. Two-dimensional gel electrophoresis demonstrated this protein to have focusing properties identical with that of a minor isoform from bovine skeletal muscle. Upon carbamylation of this bacterially expressed protein, a train of charged proteins with charge differences of -1 were produced. These carbamylated proteins were shown to have similar focusing mobilities to the Hsp70 isoforms isolated from bovine skeletal muscle. These results demonstrate the identification of a skeletal-muscle inducible Hsp70 gene and suggest that the presence of multiple Hsp70 isoforms may be the product of post-translational modifications to the Hsp70 proteins.

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Selected References

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