Abstract
Dystrophin, the product of Duchenne muscular dystrophy (DMD) gene, was purified to 70-80% homogeneity from rabbit skeletal muscle myofibrils by hydroxylapatite, wheat germ agglutinin-agarose, and DE 52 column chromatography. Rotary shadowed image of dystrophin molecules was dumpbell-shaped dimer, 100-120nm long. There were frequently linear aggregates of the dumpbell dimer.
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