The distribution of collagen fibers of rat masticatory muscles during the postnatal period (two weeks), was investigated by electrophoresis and immunohistochemistry. At these stages, the myosin of rat masticatory muscles displays specific electrophoretic patterns. Comparison of the myosin patterns of these muscles allows their identification.
1) Analysis by SDS-PAGE indicated that one of three weakly reactive stainable proteins with lower mobility than the heavy chain of myosin disappeared from the temporal muscle on day 13, as compared with other masticatory muscles. However, in histochemical analysis of the muscle fibers, the reaction specific for succinic dehydrogenase (SDH) activity was strong, and the fibers on day 13 could be classified into two types with respect to SDH activity. By contrast, on day 0, the fibers were classified into two types with respect to myosin ATPase activity.
2) Immunohistochemical analysis indicated that the distribution of the components of the extracellular matrix in the epimysium (type I collagen), perimysium (type I collagen, fibronectin, and laminin) and endomysium (type III collagen, fibronectin, laminin, and tenascin) was related to the metabolic capacity on days 12 to 13. The variability in the types of myosin and in proteins of the extracellular matrix might be important during the development of rat masticatory muscles.