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Human muscle proteins

Analysis by two-dimensional electrophoresis

Molecular Anatomy Program, Division of Biological and Medical Research (Drs. Giometti and Anderson), Argonne National Laboratory, Argonne, IL, and the Neurology Department (Dr. Danon), University of Illinois Medical Center, Chicago.

Proteins from single frozen sections of human muscle were separated by two-dimensional gel electrophoresis and detected by fluorography or Coomassie Blue staining. The major proteins were identical in different normal muscles obtained from either sex at different ages, and in Duchenne and myotonic dystrophy samples. Congenital myopathy, denervation atrophy, polymyositis, and Becker's muscular dystrophy samples, however, showed abnormal myosin light chain compositions, some with a decrease of fast-fiber myosin light chains and others with a decrease of slow-fiber light chains. These protein alterations did not correlate with any specific disease, and may be caused by generalized muscle-fiber damage.

Address correspondence and reprint requests to Dr. Giometti, Molecular Anatomy Program, Division of Biological and Medical Research, Argonne National Laboratory, Argonne, IL 60612.

This work is supported by the US Department of Energy under contract No. W-31–109-ENG-38.

Presented in part at the thirty-fourth annual meeting of the American Academy of Neurology, Washington, DC, April 1982.

Accepted for publication January 6, 1983.