Does Phosphoryiation of Myosin Light Chain Have Direct Relation to Regulation in Smooth Muscle?1
- 1 December 1977
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 82 (6), 1789-1791
- https://doi.org/10.1093/oxfordjournals.jbchem.a131878
Abstract
The phosphorylation and dephosphorylation of 20,000 molecular weight light chain of myosin has no appreciable effect on the actin-myosin-ATP interaction in vertebrate smooth muscle.This publication has 8 references indexed in Scilit:
- Phosphorylation and Dephosphorylation of a Light Chain of the Chicken Gizzard Myosin Molecule12The Journal of Biochemistry, 1977
- Regulation of the actin-myosin interaction in vertebrate smooth muscle: Activation via a myosin light-chain kinase and the effect of tropomyosinJournal of Molecular Biology, 1977
- Ca‐Linked Phosphorylation of a Light Chain of Vertebrate Smooth‐Muscle MyosinEuropean Journal of Biochemistry, 1977
- Essential Factor of Gizzard “Troponin” FractionThe Journal of Biochemistry, 1977
- Effect of phosphorylation of smooth muscle myosin on actin activation and Ca2+ regulation.Proceedings of the National Academy of Sciences, 1977
- Myosin light-chain phosphataseBiochemical Journal, 1976
- The effect of phosphorylation of gizzard myosin on actin activationBiochemical and Biophysical Research Communications, 1976
- A relationship between Ca2+ sensitivity and phosphorylation of gizzard actomyosinBiochemical and Biophysical Research Communications, 1976