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HSP70‐related proteins in bovine skeletal muscle
Author(s) -
Guerriero Vince,
Raynes Deborah A.,
Gutierrez Jesus A.
Publication year - 1989
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041400310
Subject(s) - skeletal muscle , gene isoform , biology , kilodalton , hsp70 , antibody , heat shock protein , microbiology and biotechnology , biochemistry , endocrinology , immunology , gene
Constitutive expression of HSP70‐related proteins was detected in a variety of bovine tissues using a specific antibody. All tissues contained a 73 kilodalton protein. A lower molecular weight form (72 kilodaltons) that co‐migrated on two‐dimensional gels with the stressed‐induced HSP70 was present in high levels in bovine skeletal muscle, but absent from rat skeletal muscle. Two‐dimensional gel analysis revealed several isoforms for both the 73 and 72 kilodalton forms. Purification of HSP70‐related proteins from bovine skeletal muscle, thymus gland and rat skeletal muscle demonstrated that the antibody recognized all the forms present in the tissue homogenates. The two proteins are similar but distinct as detected by one‐dimensional peptide mapping. The lower molecular form was not present in fetal tissue but was detectable in newborn animals, suggesting that the levels are regulated during development.