Clinical Chemistry
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Clinical Chemistry 26: 1152-1155, 1980;
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Clinical Chemistry, Vol 26, 1152-1155, Copyright © 1980 by American Association for Clinical Chemistry

Muscle protein analysis. II. Two-dimensional electrophoresis of normal and diseased human skeletal muscle

CS Giometti, M Barany, MJ Danon and NG Anderson

We used high-resolution two-dimensional electrophoresis to analyze the major proteins of normal and pathological human-muscle samples. The normal human-muscle pattern contains four myosin light chains: three that co-migrate with the myosin light chains from rabbit fast muscle (extensor digitorum longus), and one that co-migrates with the light chain 2 from rabbit slow muscle (soleus). Of seven Duchenne muscular dystrophy samples, four yielded patterns with decreased amounts of actin and myosin relative to normal muscle, while three samples gave patterns comparable to that for normal muscle. Six samples from patients with myotonic dystrophy also gave normal patterns. In nemaline rod myopathy, in contrast, the pattern was deficient in two of the fast- type myosin light chains.


The following articles in journals at HighWire Press have cited this article:


Home page
 Arch NeurolHome page
M. J. Danon, C. S. Giometti, J. R. Manaligod, O. H. Perurena, and J. L. Skosey
Adult-Onset Nemaline Rods in a Patient Treated for Suspected Dermatomyositis: Study With Two-Dimensionaln Electrophoresis
Arch Neurol, December 1, 1981; 38(12): 761 - 766.
[Abstract] [PDF]


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Copyright © 1980 by the American Association for Clinical Chemistry.