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Abstract
The protein product of the human Duchenne muscular dystrophy locus (DMD) and its mouse
homolog (mDMD) have been identified by using polyclonal antibodies directed against
fusion proteins containing two distinct regions of the mDMD cDNA. The DMD protein
is shown to be approximately 400 kd and to represent approximately 0.002% of total
striated muscle protein. This protein is also detected in smooth muscle (stomach).
Muscle tissue isolated from both DMD-affected boys and mdx mice contained no detectable
DMD protein, suggesting that these genetic disorders are homologous. Since mdx mice
present no obvious clinical abnormalities, the identification of the mdx mouse as
an animal model for DMD has important implications with regard to the etiology of
the lethal DMD phenotype. We have named the protein dystrophin because of its identification
via the isolation of the Duchenne muscular dystrophy locus.