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

Journal Article · Tue Jul 01 04:00:00 EDT 1980 · Clin. Chem.; (United States)

OSTI ID:5072670

Giometti, C S ^[1]; Barany, M; Danon, M J; Anderson, N G

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1. Argonne National Lab., IL

High-resolution two-dimensional electrophoresis was used 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.

• DOE Contract Number: W-31109-ENG-38
• OSTI ID: 5072670
• Journal Information: Clin. Chem.; (United States), Journal Name: Clin. Chem.; (United States) Vol. 26:8; ISSN CLCHA
• Country of Publication: United States
• Language: English

Related Subjects

37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
400102 -- Chemical & Spectral Procedures
550200 -- Biochemistry
550900* -- Pathology
59 BASIC BIOLOGICAL SCIENCES
ANIMALS
CHEMICAL ANALYSIS
DISEASES
ELECTROPHORESIS
GLOBULINS
MAMMALS
MAN
MUSCLES
MYOSIN
ORGANIC COMPOUNDS
PATHOLOGICAL CHANGES
PRIMATES
PROTEINS
VERTEBRATES