Electron Microscopic Studies of Myosin Molecules from Chicken Gizzard Muscle II: The Effect of Thiophosphorylation of the 20K-Dalton Light Chain on the ATP-Induced Change in the Conformation of Myosin Monomers1
- 1 October 1983
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 94 (4), 1147-1154
- https://doi.org/10.1093/oxfordjournals.jbchem.a134459
Abstract
The conformation of thiophosphorylated myosin molecules of chicken gizzard muscle was studied by electron microscopy with the rotary shadowing technique and by the light scattering method.Keywords
This publication has 8 references indexed in Scilit:
- A bent monomeric conformation of myosin from smooth muscle.Proceedings of the National Academy of Sciences, 1982
- Electron Microscopic Studies of Myosin Molecules from Chicken Gizzard Muscle I: The Formation of the Intramolecular Loop in the Myosin Tail1The Journal of Biochemistry, 1982
- Adenosine Triphosphate-Induced Reversible Change in the Conformation of Chicken Gizzard Myosin and Heavy Meromyosin1The Journal of Biochemistry, 1982
- Elementary Steps in the F-Actin Activated Mg2+-ATPase Reaction of Gizzard H-Meromyosin: Effects of Phosphorylation of the Light-Chain Subunit1The Journal of Biochemistry, 1981
- Rotary shadowing of extended molecules dried from glycerolJournal of Ultrastructure Research, 1980
- Roles of calcium and phosphorylation in the regulation of the activity of gizzard myosinBiochemistry, 1978
- Calcium Sensitivity of Contractile Proteins from Chicken Gizzard Muscle1The Journal of Biochemistry, 1978
- Adenosine Triphosphatase Activity and “Thick Filament” Formation of Chicken Gizzard Myosin in Low Salt Media1The Journal of Biochemistry, 1978