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Congenital nemaline myopathy. II. Quantitative changes in α‐actinin and myosin in skeletal muscle
Author(s) -
Stuhlfauth Ingo,
Jennekens Frans G. I.,
Willemse Jacobus,
Jockusch Brigitte M.
Publication year - 1983
Publication title -
muscle and nerve
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.025
H-Index - 145
eISSN - 1097-4598
pISSN - 0148-639X
DOI - 10.1002/mus.880060112
Subject(s) - nemaline myopathy , myosin , skeletal muscle , myopathy , actin , chemistry , myh7 , gel electrophoresis , myosin light chain kinase , biology , microbiology and biotechnology , endocrinology , biochemistry , genetics
Skeletal muscle obtained from 2 patients with congenital nemaline myopathy (CNM) and from a healthy control was analyzed by 1‐ and 2‐ dimensional gel electrophoresis. In total extracts, an increase of α‐actinin by a factor of 2:3 was found for CNM muscle as compared with the control. One‐ and two‐dimensional gels revealed the presence of LC F 3, the smallest light chain associated with type 2 (fast) myosin in total extracts of normal control of mixed fiber type. Both CNM samples showed the absence of this polypeptide. This result is consistent with the finding that muscle of the 2 patients exhibited nearly exclusively the ATPase activity indicative of type 1 (slow) myosin.