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NEUROLOGY 1985;35:1360
© 1985 American Academy of Neurology

Slow myosin heavy chain isozyme in nemaline myopathy

Donatella Biral, DScB, Ernesto Damiani, MD, Alfredo Margreth, MD, Elio Scarpini, MD and Guglielmo Scarlato, MD

From the National Research Council Center for Muscle Biology and Physiopathology, Institute of General Pathology (Drs. Riral, Damiani, and Margreth), University of Padova, Padova; and the Institute of Neurology (Drs. Scarpini and Scarlato), University of Milano, Milano, Italy.

Muscle biopsies from two sporadic cases of congenital nemaline myopathy were examined for myosin heavy chain composition. Electrophoresis of congenital nemaline myopathy (CNM) muscle myosin in SDS-5% polyacrylamide gels gave rise to a single heavy chain band, with a migration rate and antigenic properties identical to that of the adult slow form, as demonstrated by Western blot techniques and by using specific antibody. Immunofluorescent studies indicate that CNM muscle fibers, including the most severely atrophic fibers, are homogeneous with respect to myosin heavy chain composition.

Address correspondence and reprint requests to Dr. Margreth, N.R.C. Center for Muscle Biology and Physiopathology, Institute of General Pathology, University of Padova, Via Loredan 16, 35131 Padova, Italy.

This work was supported by institutional funds from the Consiglio Nazionale delle Ricerche and in part by grant to A.M. from Legato Din0 Ferrari.

Accepted for publication December 7, 1984.






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