抄録
The effects of tropomyosin (TM) on the stability of actin with and without heavy meromyosin (HMM) during storage at low temperature were studied by the DNase I inhibition assay. The stabilizing effect of TM on actin without ATP at 0°C was associated with the extent of binding of TM to the actin filaments that was dependent on the KCl concentrations: i.e., TM effectively depressed the denaturation of actin at a KCl concentration ranging from 0.1 to 0.5 M whereby TM can be bound to F-actin, Stabilization by TM could reduce the probability of the destabilization of actin due to a small amount of HMM. A combination of TM and a large amount of HMM strongly stabilized actin, even in a high salt concentration such as 0.6 M KCl These results indicate that tropomyosin played an important role in stabilizing actin in an actomyosin complex (natural actomyosin) during treatment with salt at a low temperature.
