Fluorescence microscope study of the binding of added C protein to skeletal muscle myofibrils

doi:10.1083/jcb.90.1.25

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Fluorescence microscope study of the binding of added C protein to skeletal muscle myofibrils

C Moos

The binding of extra C protein to rabbit skeletal muscle myofibrils has been investigated by fluorescence microscopy with fluorescein-labeled C protein or unmodified C protein plus fluorescein-labeled anti-C protein. Added C protein binds strongly to the I bands, which is consistent with its binding to F actin in solution (Moos, C., C. M. Mason, J. M. Besterman, I. M. Feng, and J. H. Dubin. 1978. J. Mol. Biol. 124:571-586). Of particular interest, the binding to the I band is calcium regulated: it requires a free calcium ion concentration comparable to that which activates the myofibrillar ATPase. This increases the likelihood that C protein-actin interaction might be physiologically significant. When I band binding is suppressed, binding in the A band becomes evident. It appears to occur particularly near the M line, and possibly at the edges of the A band as well, suggesting that those parts of the thick filaments that lack C protein in vivo may nevertheless be capable of binding added C protein.
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