The effect of adrenaline on the phosphorylation of the P light chain of myosin and troponin I in the perfused rabbit heart
- 1 July 1981
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 197 (1), 185-193
- https://doi.org/10.1042/bj1970185
Abstract
1. Two-dimensional electrophoresis has been used to study the extent of phosphorylation of the P light chain of myosin and troponin I in the rabbit beating heart. 2. A procedure has been developed that eliminates endogenous protein phosphatase activity during homogenization and sample preparation for electrophoresis. 3. Evidence has been obtained for two unphosphorylated forms of the P light chain in myosin from the ventricle of the rabbit, guinea pig and cow. 4. In vivo and in the rabbit perfused beating heart about 25% of the P light-chain fraction is in the phosphorylated form. 5. Intervention with adrenaline produced a slight increase in the extent of phosphorylation that reached a maximum after the peak in inotropic response. A similar increase was obtained with ischaemia in the absence of adrenaline. 6. The changes in phosphorylation of the major forms of troponin I identified by electrophoresis occurred after the peak of response to adrenaline and were compatible with previous results.This publication has 22 references indexed in Scilit:
- Changes in phosphorylation of P light chain of myosin in perfused rabbit heartNature, 1976
- Myosin light-chain phosphataseBiochemical Journal, 1976
- The relationship between biological activity and primary structure of troponin I from white skeletal muscle of the rabbitBiochemical Journal, 1976
- Phosphorylation of the light-chain components of myosin from cardiac and red skeletal musclesBiochemical Journal, 1975
- Tentative identification of the amino acid that binds tyrosine as a single unit into a soluble brain proteinFEBS Letters, 1975
- Phosphorylation of troponin and the effects of interactions between the components of the complexBiochemical Journal, 1974
- Myosin light‐chain kinase, a new enzyme from striated muscleFEBS Letters, 1974
- Phosphorylation of the ‘37000 component’ of the troponin complex (troponin-T)Biochemical Journal, 1973
- An electrophoretic study of the low-molecular-weight components of myosinBiochemical Journal, 1970
- The Specific Precipitation of Orthophosphate and Some Biochemical ApplicationsJournal of Biological Chemistry, 1964