Non-uniform staining of myofibril a bands by a monoclonal antibody to skeletal muscle myosin S1 heavy chain.

A monoclonal antibody specific for the S1 fragment of skeletal muscle myosin has been identified. The antibody does not inhibit actin-activated Mg2+-ATPase or K+-EDTA-activated ATPase of myosin, indicating that it is not related to the portion of the S1 which carries the ATPase activity. In the absence of relaxing medium, antibody binding to the myosin filament is restricted to narrow regions on each side of the bare zone region of the filament, and to a narrow region at the tapered ends of the filament. This restricted antibody binding is not altered by the attachment of the myosin cross-bridges to the actin filaments. In the presence of relaxing medium, antibody binding occurs along the entire length of the cross-bridge-bearing region of the filament. The restricted binding to only small regions of the filament in the absence of relaxing medium suggests that the molecular packing of the myosin in different portions of the filament may be different, resulting in differences in the availability of the antigenic site on the S1 for antibody binding. The change in availability of the antigenic sites along the filament in the presence of relaxing medium may reflect a perturbation in the molecular packing of the filament, or a conformational change resulting from the binding of MgATP, both of which could affect the availability of the antigenic sites on the S1 for antibody.