| Abstract: | The hypothesis that an alteration in the SH1 site of hypertrophy myosin is reponsible for the reduced Ca2+-stimulated ATPase activity is examined.The functional integrity of the SH1 site was evaluated by measurement of the (K+)-EDTA-stimulated and Mg2+-inhibited ATPase activities. Neither activity differed from control although the Ca2+-stimulated ATPase of the same preparations was significantly reduced. The reduction in Ca2+-activated ATPase was independent of ionic strength. Titration with N-ethylmaleimide elevated the Ca2+-stimulated ATPase of hypertrophy myosin to the same peak activity as control. Actin-stimulated ATPase activity of hypertrophy myosin was also reduced. The results indicate that the SH1 of hypertrophy myosin is functionally intact for (K+)EDTA-stimulated ATPase and Mg2+ inhibition, but functionally deficient with regard to Ca2+-stimulated and actin-activated ATPase activities. This implies a partition of the functional aspects of SH1. |
