Publication | Open Access
Myosin Adenosine Triphosphatase
211
Citations
12
References
1974
Year
Molecular BiologyCytoskeletonCellular PhysiologySkeletal MuscleMyosin MgatpaseCell PhysiologyMolecular PhysiologyBiochemistryMechanism Of ActionIonic StrengthProtein PhosphorylationSignal TransductionNatural SciencesPhysiologyIonic Strength DependenceCell MotilityCellular BiochemistryMedicineMyosin Adenosine Triphosphatase
Abstract The ionic strength dependence of the absolute activation of myosin MgATPase by actin binding or by chemical modification of the SH1 sulfhydryl group has been investigated. At physiological ionic strengths the extent of activation induced by the two procedures are essentially identical, but differ markedly as the ionic strength is decreased below 0.10. Similar behavior is also found for subfragment I. These findings are discussed in terms of the mechanism of actin activation of myosin MgATPase under physiological conditions.
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