The C-terminus of the myosin rod is a key domain involved in regulating myosin interactions and solubility.
Antibody effects on myosin solubility remain preclinical; leaves open C-terminal domain roles in cardiac filament regulation.
Monoclonal antibody Fab fragments which bind epitopes in the rod domain of skeletal muscle myosin had specific effects on the solubility properties of chicken muscle myosin in vitro. Two antibodies (NA4 and 5C3), which bind at the C-terminal portion of the rod domain caused myosin to remain soluble and monomeric in 0.1 M KCl, pH 7.2, conditions in which myosin normally aggregates into filamentous structures. Other antibodies (EB165 and AB8), which bind in the middle of the rod did not alter either myosin solubility or the morphology of the myosin assemblies formed. These results demonstrate the importance of the C-terminus of the myosin rod as a domain involved in regulating myosin interactions and solubility.
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Wick et al. (1996) studied this question.
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