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August 1972

Myosin From Normal and Dystrophic Human Muscle: Immunochemical and Electrophoretic Studies

Author Affiliations

From the Spiller Neurological Unit and Department of Neurology, Hospital of the University of Pennsylvania, and the Department of Neurology, Philadelphia General Hospital, Philadelphia.

Arch Neurol. 1972;27(2):159-173. doi:10.1001/archneur.1972.00490140063010

Myosin was isolated from normal human skeletal muscle. After purification, there was virtually no actin, adenylate deaminase, or myokinase. Ribonucleoprotein was more tenacious than in preparations of rabbit myosin but could be eliminated by chromatography on diethylaminoethyl cellulose. The enzymatic properties of myosin from human skeletal muscle were more like that from red muscle than white muscle. Techniques were developed for electrophoresis of myosin in pyrophosphate buffer on agarose and 4% acrylamide gels. Immunodiffusion analysis, using antisera prepared to normal myosin, and electrophoretic methods were sensitive enough to detect differences between myosins from some species and from human heart and uterus. However, there was no difference between myosin from normal human muscle and the protein from patients with the major forms of muscular dystrophy (Duchenne, facioscapulohumeral, limb-girdle, myotonic).

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