Kinetic studies with synthetic myosin minifilaments show the equivalence of actomyosin and acto-HMM ATPases.
Open Access
- 1 October 1980
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 255 (20) , 9541-9544
- https://doi.org/10.1016/s0021-9258(18)43424-2
Abstract
No abstract availableThis publication has 18 references indexed in Scilit:
- All myosin heads form bonds with actin in rigor rabbit skeletal muscleBiochemistry, 1980
- On the question of co-operative interaction of myosin heads with F-actin in the presence of ATPJournal of Molecular Biology, 1980
- Studies on the Actin Activation of Myosin Subfragment‐1 Isoenzymes and the Role of Myosin Light ChainsEuropean Journal of Biochemistry, 1979
- Mechanism of Actomyosin Atpase and the Problem of Muscle ContractioCRC Critical Reviews in Biochemistry, 1979
- Interaction of myosin subfragments with F-actinBiochemistry, 1978
- Effect of actin concentration on the intermediate oxygen exchange of myosin; relation to the refractory state and the mechanism of exchangeBiochemistry, 1978
- The reaction of myosin with N-ethylmaleimide in the presence of ADPBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1974
- Substructure of the myosin molecule: IV. Interactions of myosin and its subfragments with adenosine triphosphate and F-actinJournal of Molecular Biology, 1973
- Effect of adenosine di- and triphosphates on the stability of synthetic myosin filamentsBiochemistry, 1972
- Self-association in the myosin system at high ionic strength. I. Sensitivity of the interaction to pH and ionic environmentBiochemistry, 1970