HSP70-related proteins in bovine skeletal muscle.
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.
Department of Animal Sciences, University of Arizona, Tucson 85721.
V
V
Guerriero
D A
DA
Raynes
J A
JA
Gutierrez
D000818:Animals; D015153:Blotting, Western; D002417:Cattle; D015180:Electrophoresis, Gel, Two-Dimensional; D006360:Heat-Shock Proteins / Q000302:isolation & purification / Q000378:metabolism*; D006358:Hot Temperature; D009124:Muscle Proteins / Q000378:metabolism; D009132:Muscles / Q000378:metabolism*; D010449:Peptide Mapping; D051381:Rats; D013950:Thymus Gland / Q000378:metabolism
D006360:Heat-Shock Proteins; D009124:Muscle Proteins