 |
|
Myosin From Normal and Dystrophic Human MuscleImmunochemical and Electrophoretic Studies
Audrey S. Penn, MD;
Ruey A. Cloak;
Lewis P. Rowland, MD
Arch Neurol. 1972;27(2):159-173.
Abstract
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).
Author Affiliations
Philadelphia
From the Spiller Neurological Unit and Department of Neurology, Hospital of the University of Pennsylvania, and the Department of Neurology, Philadelphia General Hospital, Philadelphia.
Footnotes
Accepted for publication Feb 19, 1972.
Reprint requests to Department of Neurology, Johnson Pavilion, University of Pennsylvania School of Medicine, Philadelphia 19104 (Dr. Penn).
 CiteULike  Connotea  Del.icio.us  Digg  Reddit  Technorati
What's this?
THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES
Pathogenesis of Muscular Dystrophies
Rowland
Arch Neurol 1976;33:315-321.
ABSTRACT
Actomyosin Alterations in Duchenne Muscular Dystrophy
Samaha
Arch Neurol 1973;28:405-407.
ABSTRACT
|
