Abstract
Purified serine protease was obtained from skeletal and heart muscle of 150-day-old myopathic hamsters. The skeletal muscle enzyme showed identical molecular weight and characteristics toward various reagents and inhibitors when compared with the cardiac muscle enzyme. In addition, no antigenic differences were detected between the two enzymes using double-immunodiffusion test. Further characterization of the properties of the two enzymes was carried out by using individual myofibrillar proteins as substrates. Both enzymes were capable of degrading myosin, tropomyosin and troponin but not actin. The divalent cations Ca 2+ or Mg 2+ were able to protect the myosin light chain 2 against proteolytic cleavage. The cellular localization of the serine protease of skeletal and cardiac muscle was studied by immunohistochemical techniques. The observations indicate that serine protease is contained within the cytoplasmic granules of cardiac and skeletal muscle mast cells of myopathic and control hamsters. The number of labeled mast cells is about three-fold greater in myopathic than in control tissues. This increase correlates with the increase in enzyme activity as detected by biochemical assay in tissue homogenates.
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