Phosphorylation of Human Platelet Myosin
- 1 November 1973
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 70 (11) , 3115-3119
- https://doi.org/10.1073/pnas.70.11.3115
Abstract
A preparation extracted from human blood platelets, which incorporates (32)P from gamma-labeled AT(32)P into one of the two light chains of platelet myosin and platelet myosin head is described. This phosphorylation, which appears to be due to an endogenous kinase, is specific for the myosin light chain in that no other protein extracted in 0.6 M KCl-15 mM Tris.HCl (pH 7.5) is phosphorylated. The phosphorylated light chain, which has been purified by gel filtration, releases the covalently bound phosphate after incubation in alkali and not after incubation in acid.Keywords
This publication has 17 references indexed in Scilit:
- A phosphorylated light-chain component of myosin from skeletal muscleBiochemical Journal, 1973
- Human platelet actin. Isolation and properties.1973
- Actomyosin-Like Protein in BrainScience, 1973
- Phosphorylation of the ‘37000 component’ of the troponin complex (troponin-T)Biochemical Journal, 1973
- Dephosphorylation of the Inhibitor Component of Troponin by Phosphorylase PhosphataseJournal of Biological Chemistry, 1972
- Cyclic AMP and Platelet FunctionNew England Journal of Medicine, 1972
- Isolation and Characterization of Myosin and Two Myosin Fragments from Human Blood PlateletsProceedings of the National Academy of Sciences, 1971
- Electrophoretic analysis of the major polypeptides of the human erythrocyte membraneBiochemistry, 1971
- Adenyl cyclase activity in human plateletsBiochemical and Biophysical Research Communications, 1969
- DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*Annals of the New York Academy of Sciences, 1964