Abstract
Myoid cells of calf and rat thymus have been identified by staining with a monoclonal antibody to the heavy chain of myosin that is not isoform specific. Heterogeneity in the protein composition of myoid cells has been demonstrated by staining with antibodies to the skeletal muscle isoforms of the myosin heavy chain, C-protein and components of the troponin complex. The immunochemical studies suggest that the myoid cells contain proteins closely resembling if not identical with those present in the myofibrils of skeletal muscle. The slow and fast skeletal muscle isoforms of the myofibrillar proteins are present in a large proportion of the myoid cells. A fraction of the myoid cells contains only the fast isoforms of the myofibrillar proteins but there is no sharp compartmentalization of the isoforms as occurs in type 1 and type 2 fibres of skeletal muscle. In general the pattern of gene expression is similar to that of developing skeletal muscle.
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